Publications

2013, 2014, 2015, 2016, 2017, 2018, 2019, 2020, 2021, 2022, 2023, 2024

Last updated: 18.12.2024

2013

Ataka, K., Stripp, S.T. and Heberle, J. (2013). Surface-enhanced infrared absorption spectroscopy (SEIRAS) to probe monolayers of membrane proteins. Biochim Biophys Acta, 1828, 10: 2283-2293 doi: http://dx.doi.org/10.1016/j.bbamem.2013.04.026
Bonthuis, D.J. and Netz, R.R. (2013). Beyond the continuum: how molecular solvent structure affects electrostatics and hydrodynamics at solid-electrolyte interfaces. J Phys Chem B, 117, 39: 11397-11413 doi: http://dx.doi.org/10.1021/jp402482q
Escobar, F.V., Utesch, T., Narikawa, R., Ikeuchi, M., Mroginski, M.A., Gartner, W. and Hildebrandt, P. (2013). Photoconversion mechanism of the second GAF domain of cyanobacteriochrome AnPixJ and the cofactor structure of its green-absorbing state. Biochemistry, 52, 29: 4871-4880 doi: http://dx.doi.org/10.1021/bi400506a
Glockner, C., Kern, J., Broser, M., Zouni, A., Yachandra, V. and Yano, J. (2013). Structural changes of the oxygen-evolving complex in photosystem II during the catalytic cycle. J Biol Chem, 288, 31: 22607-22620 doi: http://dx.doi.org/10.1074/jbc.M113.476622
Kern, J., Alonso-Mori, R., Tran, R., Hattne, J., Gildea, R.J., Echols, N., Glöckner, C., Hellmich, J., Laksmono, H., Sierra, R.G., Lassalle-Kaiser, B., Koroidov, S., Lampe, A., Han, G.Y., Gul, S., DiFiore, D., Milathianaki, D., Fry, A.R., Miahnahri, A., Schafer, D.W., Messerschmidt, M., Seibert, M.M., Koglin, J.E., Sokaras, D., Weng, T.C., Sellberg, J., Latimer, M.J., Grosse-Kunstleve, R.W., Zwart, P.H., White, W.E., Glatzel, P., Adams, P.D., Bogan, M.J., Williams, G.J., Boutet, S., Messinger, J., Zouni, A., Sauter, N.K., Yachandra, V.K., Bergmann, U. and Yano, J. (2013). Simultaneous Femtosecond X-ray Spectroscopy and Diffraction of Photosystem II at Room Temperature. Science, 340, 6131: 491-495 doi: http://dx.doi.org/10.1126/science.1234273
Kirchberg, K., Michel, H. and Alexiev, U. (2013). Exploring the entrance of proton pathways in cytochrome c oxidase from Paracoccus denitrificans: surface charge, buffer capacity and redox-dependent polarity changes at the internal surface. Biochim Biophys Acta, 1827, 3: 276-284 doi: http://dx.doi.org/10.1016/j.bbabio.2012.10.014
Kozuch, J., von der Hocht, I., Hilbers, F., Michel, H. and Weidinger, I.M. (2013). Resonance Raman characterization of the ammonia-generated oxo intermediate of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry, 52, 36: 6197-6202 doi: http://dx.doi.org/10.1021/bi400535m
Krause, N., Engelhard, C., Heberle, J., Schlesinger, R. and Bittl, R. (2013). Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy. FEBS Lett, 587, 20: 3309-3313 doi: http://dx.doi.org/10.1016/j.febslet.2013.08.043
Linke, M., Yang, Y., Zienicke, B., Hammam, M.A.S., von Haimberger, T., Zacarias, A., Inomata, K., Lamparter, T. and Heyne, K. (2013). Electronic transitions and heterogeneity of the bacteriophytochrome Pr absorption band: An angle balanced polarization resolved femtosecond VIS pump-IR probe study. Biophys J, 105, 8: 1756-1766 doi: http://dx.doi.org/10.1016/j.bpj.2013.08.041
Lórenz-Fonfría, V.A., Resler, T., Krause, N., Nack, M., Gossing, M., Fischer von Mollard, G., Bamann, C., Bamberg, E., Schlesinger, R. and Heberle, J. (2013). Transient protonation changes in channelrhodopsin-2 and their relevance to channel gating. Proc Natl Acad Sci U S A, 110, 14: E1273-E1281 doi: http://dx.doi.org/10.1073/pnas.1219502110
Mamatkulov, S., Fyta, M. and Netz, R.R. (2013). Force fields for divalent cations based on single-ion and ion-pair properties. J Chem Phys, 138, 2: 12 doi: http://dx.doi.org/10.1063/1.4772808
Müh, F. and Zouni, A. (2013). The nonheme iron in photosystem II. Photosynth Res, 116, 2-3: 295-314 doi: http://dx.doi.org/10.1007/s11120-013-9926-y
Neumann-Verhoefen, M.K., Neumann, K., Bamann, C., Radu, I., Heberle, J., Bamberg, E. and Wachtveitl, J. (2013). Ultrafast Infrared Spectroscopy on Channelrhodopsin-2 Reveals Efficient Energy Transfer from the Retinal Chromophore to the Protein. J Am Chem Soc, 135, 18: 6968-6976 doi: http://dx.doi.org/10.1021/ja400554y
Ritter, E., Piwowarski, P., Hegemann, P. and Bartl, F.J. (2013). Light-dark adaptation of channelrhodopsin C128T mutant. J Biol Chem, 288, 15: 10451-10458 doi: http://dx.doi.org/10.1074/jbc.M112.446427
Salewski, J., Escobar, F.V., Kaminski, S., von Stetten, D., Keidel, A., Rippers, Y., Michael, N., Scheerer, P., Piwowarski, P., Bartl, F., Frankenberg-Dinkel, N., Ringsdorf, S., Gärtner, W., Lamparter, T., Mroginski, M.A. and Hildebrandt, P. (2013). Structure of the Biliverdin Cofactor in the Pfr State of Bathy and Prototypical Phytochromes. J Biol Chem, 288, 23: 16800-16814 doi: http://dx.doi.org/10.1074/jbc.M113.457531
Schneider, F., Gradmann, D. and Hegemann, P. (2013). Ion Selectivity and Competition in Channelrhodopsins. Biophys J, 105, 1: 91-100 doi: http://dx.doi.org/10.1016/j.bpj.2013.05.042
Vogt, A., Wietek, J. and Hegemann, P. (2013). Gloeobacter Rhodopsin, Limitation of Proton Pumping at High Electrochemical Load. Biophys J, 105, 9: 2055-2063 doi: http://dx.doi.org/10.1016/j.bpj.2013.08.031
von Hansen, Y., Gekle, S. and Netz, R.R. (2013). Anomalous Anisotropic Diffusion Dynamics of Hydration Water at Lipid Membranes. Phys Rev Lett, 111, 11: 5 doi: http://dx.doi.org/10.1103/PhysRevLett.111.118103
Woelke, A.L., Kuehne, C., Meyer, T., Galstyan, G., Dernedde, J. and Knapp, E.W. (2013). Understanding Selectin Counter-Receptor Binding from Electrostatic Energy Computations and Experimental Binding Studies. J Phys Chem B, 117, 51: 16443-16454 doi: http://dx.doi.org/10.1021/jp4099123
Zienicke, B., Molina, I., Glenz, R., Singer, P., Ehmer, D., Escobar, F.V., Hildebrandt, P., Diller, R. and Lamparter, T. (2013). Unusual spectral properties of bacteriophytochrome Agp2 result from a deprotonation of the chromophore in the red-absorbing form Pr. J Biol Chem, 288, 44: 31738-31751 doi: http://dx.doi.org/10.1074/jbc.M113.479535

2014 back up ↑

Alexiev, U. and Farrens, D.L. (2014). Fluorescence spectroscopy of rhodopsins: insights and approaches. Biochim Biophys Acta, 1837, 5: 694-709 doi: http://dx.doi.org/10.1016/j.bbabio.2013.10.008
AzimiHashemi, N., Erbguth, K., Vogt, A., Riemensperger, T., Rauch, E., Woodmansee, D., Nagpal, J., Brauner, M., Sheves, M., Fiala, A., Kattner, L., Trauner, D., Hegemann, P., Gottschalk, A. and Liewald, J.F. (2014). Synthetic retinal analogues modify the spectral and kinetic characteristics of microbial rhodopsin optogenetic tools. Nat Commun, 5, 5810 doi: http://dx.doi.org/10.1038/ncomms6810
Bommer, M., Kunze, C., Fesseler, J., Schubert, T., Diekert, G. and Dobbek, H. (2014). Structural basis for organohalide respiration. Science, 346, 6208: 455-458 doi: http://dx.doi.org/10.1126/science.1258118
Brecht, M., Skandary, S., Hellmich, J., Glöckner, C., Konrad, A., Hussels, M., Meixner, A.J., Zouni, A. and Schlodder, E. (2014). Spectroscopic properties of photosystem II core complexes from Thermosynechococcus elongatus revealed by single-molecule experiments. Biochim Biophys Acta, 1837, 6: 773-781 doi: http://dx.doi.org/10.1016/j.bbabio.2014.01.025
del Val, C., Bondar, L. and Bondar, A.N. (2014). Coupling between inter-helical hydrogen bonding and water dynamics in a proton transporter. J Struct Biol, 186, 1: 95-111 doi: http://dx.doi.org/10.1016/j.jsb.2014.02.010
del Val, C., Royuela-Flor, J., Milenkovic, S. and Bondar, A.N. (2014). Channelrhodopsins: A bioinformatics perspective. Biochim Biophys Acta, 1837, 5: 643-655 doi: http://dx.doi.org/10.1016/j.bbabio.2013.11.005
Ernst, O.P., Lodowski, D.T., Elstner, M., Hegemann, P., Brown, L.S. and Kandori, H. (2014). Microbial and animal rhodopsins: structures, functions, and molecular mechanisms. Chem Rev, 114, 1: 126-163 doi: http://dx.doi.org/10.1021/cr4003769
Escobar, F.V., Hildebrandt, T., Utesch, T., Schmitt, F.J., Seuffert, I., Michael, N., Schulz, C., Mroginski, M.A., Friedrich, T. and Hildebrandt, P. (2014). Structural Parameters Controlling the Fluorescence Properties of Phytochromes. Biochemistry, 53, 1: 20-29 doi: http://dx.doi.org/10.1021/bi401287u
Gekle, S. and Netz, R.R. (2014). Nanometer-Resolved Radio-Frequency Absorption and Heating in Biomembrane Hydration Layers. J Phys Chem B, 118, 18: 4963-4969 doi: http://dx.doi.org/10.1021/jp501562p
Heberle, J., Deupi, X. and Schertler, G. (2014). Retinal proteins - You can teach an old dog new tricks Foreword. Biochim Biophys Acta, 1837, 5: 531-532 doi: http://dx.doi.org/10.1016/j.bbabio.2014.02.019
Hellmich, J., Bommer, M., Burkhardt, A., Ibrahim, M., Kern, J., Meents, A., Müh, F., Dobbek, H. and Zouni, A. (2014). Native-like Photosystem II Superstructure at 2.44 Å Resolution through Detergent Extraction from the Protein Crystal. Structure, 22, 11: 1607-1615 doi: http://dx.doi.org/10.1016/j.str.2014.09.007
Karge, O., Bondar, A.N. and Dau, H. (2014). Cationic screening of charged surface groups (carboxylates) affects electron transfer steps in photosystem-II water oxidation and quinone reduction. Biochim Biophys Acta, 1837, 10: 1625-1634 doi: http://dx.doi.org/10.1016/j.bbabio.2014.07.012
Kern, J., Tran, R., Alonso-Mori, R., Koroidov, S., Echols, N., Hattne, J., Ibrahim, M., Gul, S., Laksmono, H., Sierra, R.G., Gildea, R.J., Han, G., Hellmich, J., Lassalle-Kaiser, B., Chatterjee, R., Brewster, A.S., Stan, C.A., Glöckner, C., Lampe, A., DiFiore, D., Milathianaki, D., Fry, A.R., Seibert, M.M., Koglin, J.E., Gallo, E., Uhlig, J., Sokaras, D., Weng, T.C., Zwart, P.H., Skinner, D.E., Bogan, M.J., Messerschmidt, M., Glatzel, P., Williams, G.J., Boutet, S., Adams, P.D., Zouni, A., Messinger, J., Sauter, N.K., Bergmann, U., Yano, J. and Yachandra, V.K. (2014). Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy. Nat Commun, 5, 11 doi: http://dx.doi.org/10.1038/ncomms5371
Lórenz-Fonfría, V.A. and Heberle, J. (2014). Channelrhodopsin unchained: structure and mechanism of a light-gated cation channel. Biochim Biophys Acta, 1837, 5: 626-642 doi: http://dx.doi.org/10.1016/j.bbabio.2013.10.014
Lórenz-Fonfría, V.A. and Heberle, J. (2014). Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy. J Vis Exp, 88: 16 doi: http://dx.doi.org/10.3791/51622
Lórenz-Fonfría, V.A., Muders, V., Schlesinger, R. and Heberle, J. (2014). Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1. J Chem Phys, 141, 22: 12 doi: http://dx.doi.org/10.1063/1.4895796
Meyer, T. and Knapp, E.W. (2014). Database of protein complexes with multivalent binding ability: Bival-bind. Proteins, 82, 5: 744-751 doi: http://dx.doi.org/10.1002/prot.24453
Mielack, C., del Val, C., Bondar, M.L. and Bondar, A.N. (2014). Proton-Coupled Water and Hydrogen-Bond Dynamics in Channelrhodopsin. Biophys J, 106, 2: 16a-17a doi: http://dx.doi.org/DOI 10.1016/j.bpj.2013.11.145
Muders, V., Kerruth, S., Lórenz-Fonfría, V.A., Bamann, C., Heberle, J. and Schlesinger, R. (2014). Resonance Raman and FTIR spectroscopic characterization of the closed and open states of channelrhodopsin-1. Febs Letters, 588, 14: 2301-2306 doi: http://dx.doi.org/10.1016/j.febslet.2014.05.019
Rinne, K.F., Gekle, S. and Netz, R.R. (2014). Dissecting ion-specific dielectric spectra of sodium-halide solutions into solvation water and ionic contributions. J Chem Phys, 141, 21: 16 doi: http://dx.doi.org/10.1063/1.4901927
Rinne, K.F., Gekle, S. and Netz, R.R. (2014). Ion-Specific Solvation Water Dynamics: Single Water versus Collective Water Effects. J Phys Chem A, 118, 50: 11667-11677 doi: http://dx.doi.org/10.1021/jp5066874
Robertazzi, A., Galstyan, A. and Knapp, E.W. (2014). Reprint of PSII Manganese Cluster: Protonation of W2, O5, O4 and His337 in the S1 state explored by combined quantum chemical and electrostatic energy computations. Biochim Biophys Acta Bioenerg, 1837, 9: 1389-1394 doi: http://dx.doi.org/10.1016/j.bbabio.2014.07.008
Robertazzi, A., Galstyan, A. and Knapp, E.W. (2014). PSII manganese cluster: protonation of W2, O5, O4 and His337 in the S1 state explored by combined quantum chemical and electrostatic energy computations. Biochim Biophys Acta, 1837, 8: 1316-1321 doi: http://dx.doi.org/10.1016/j.bbabio.2014.03.018
Rose, A.S., Elgeti, M., Zachariae, U., Grubmüller, H., Hofmann, K.P., Scheerer, P. and Hildebrand, P.W. (2014). Position of Transmembrane Helix 6 Determines Receptor G Protein Coupling Specificity. J Am Chem Soc, 136, 32: 11244-11247 doi: http://dx.doi.org/10.1021/ja5055109
Sedlmeier, F., Shadkhoo, S., Bruinsma, R. and Netz, R.R. (2014). Charge/mass dynamic structure factors of water and applications to dielectric friction and electroacoustic conversion. J Chem Phys, 140, 5: 11 doi: http://dx.doi.org/10.1063/1.4863444
Sugihara, M., Suwa, M. and Bondar, A.N. (2014). Dynamics of bovine opsin bound to G-protein fragments. J Struct Biol, 188, 1: 79-86 doi: http://dx.doi.org/10.1016/j.jsb.2014.08.001
Tran, R., Kern, J., Hattne, J., Koroidov, S., Hellmich, J., Alonso-Mori, R., Sauter, N.K., Bergmann, U., Messinger, J., Zouni, A., Yano, J. and Yachandra, V.K. (2014). The Mn₄Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser. Philos Trans R Soc B-Biol Sci, 369, 1647: 6 doi: http://dx.doi.org/10.1098/rstb.2013.0324
Wietek, J., Wiegert, J.S., Adeishvili, N., Schneider, F., Watanabe, H., Tsunoda, S.P., Vogt, A., Elstner, M., Oertner, T.G. and Hegemann, P. (2014). Conversion of Channelrhodopsin into a Light-Gated Chloride Channel. Science, 344, 6182: 409-412 doi: http://dx.doi.org/10.1126/science.1249375
Woelke, A.L., Galstyan, G. and Knapp, E.W. (2014). Lysine 362 in cytochrome c oxidase regulates opening of the K-channel via changes in pKA and conformation. Biochim Biophys Acta, 1837, 12: 1998-2003 doi: http://dx.doi.org/10.1016/j.bbabio.2014.08.003
Woelke, A.L., Wagner, A., Galstyan, G., Meyer, T. and Knapp, E.W. (2014). Proton transfer in the K-channel analog of B-type Cytochrome c oxidase from Thermus thermophilus. Biophys J, 107, 9: 2177-2184 doi: http://dx.doi.org/10.1016/j.bpj.2014.09.010
Yang, Y., Linke, M., von Haimberger, T., Matute, R., Gonzalez, L., Schmieder, P. and Heyne, K. (2014). Active and silent chromophore isoforms for phytochrome Pr photoisomerization: An alternative evolutionary strategy to optimize photoreaction quantum yields. Struct Dyn, 1, 1: 014701 doi: http://dx.doi.org/10.1063/1.4865233

2015 back up ↑

Bruun, S., Stoeppler, D., Keidel, A., Kuhlmann, U., Luck, M., Diehl, A., Geiger, M.A., Woodmansee, D., Trauner, D., Hegemann, P., Oschkinat, H., Hildebrandt, P. and Stehfest, K. (2015). Light-Dark Adaptation of Channelrhodopsin Involves Photoconversion between the all-trans and 13-cis Retinal Isomers. Biochemistry, 54, 35: 5389-5400 doi: http://dx.doi.org/10.1021/acs.biochem.5b00597
Escobar, F.V., Piwowarski, P., Salewski, J., Michael, N., Fernandez Lopez, M., Rupp, A., Qureshi, B.M., Scheerer, P., Bartl, F., Frankenberg-Dinkel, N., Siebert, F., Andrea Mroginski, M. and Hildebrandt, P. (2015). A protonation-coupled feedback mechanism controls the signalling process in bathy phytochromes. Nat Chem, 7, 5: 423-430 doi: http://dx.doi.org/10.1038/nchem.2225
Escobar, F.V., von Stetten, D., Gunther-Lutkens, M., Keidel, A., Michael, N., Lamparter, T., Essen, L.O., Hughes, J., Gartner, W., Yang, Y., Heyne, K., Mroginski, M.A. and Hildebrandt, P. (2015). Conformational heterogeneity of the Pfr chromophore in plant and cyanobacterial phytochromes. Front Mol Biosci, 2, 37 doi: http://dx.doi.org/10.3389/fmolb.2015.00037
Galstyan, G. and Knapp, E.W. (2015). Computing pK(A) values of hexa-aqua transition metal complexes. J Comput Chem, 36, 2: 69-78 doi: http://dx.doi.org/10.1002/jcc.23764
Graf, D., Wesslowski, J., Ma, H., Scheerer, P., Krauss, N., Oberpichler, I., Zhang, F. and Lamparter, T. (2015). Key Amino Acids in the Bacterial (6-4) Photolyase PhrB from Agrobacterium fabrum. Plos One, 10, 10: 14 doi: http://dx.doi.org/10.1371/journal.pone.0140955
Guerra, F., Adam, S. and Bondar, A.N. (2015). Revised force-field parameters for chlorophyll-a, pheophytin-a and plastoquinone-9. J Mol Graph, 58, 30-39 doi: http://dx.doi.org/10.1016/j.jmgm.2015.03.001
Guerra, F. and Bondar, A.N. (2015). Dynamics of the Plasma Membrane Proton Pump. J Membr Biol, 248, 3: 443-453 doi: http://dx.doi.org/10.1007/s00232-014-9732-2
Ibrahim, M., Chatterjee, R., Hellmich, J., Tran, R., Bommer, M., Yachandra, V.K., Yano, J., Kern, J. and Zouni, A. (2015). Improvements in serial femtosecond crystallography of photosystem II by optimizing crystal uniformity using microseeding procedures. Struct Dyn-US, 2, 4: 11 doi: http://dx.doi.org/10.1063/1.4919741
Kielb, P., Sezer, M., Katz, S., Lopez, F., Schulz, C., Gorton, L., Ludwig, R., Wollenberger, U., Zebger, I. and Weidinger, I.M. (2015). Spectroscopic Observation of Calcium-Induced Reorientation of Cellobiose Dehydrogenase Immobilized on Electrodes and its Effect on Electrocatalytic Activity. ChemPhysChem, 16, 9: 1960-1968 doi: http://dx.doi.org/10.1002/cphc.201500112
Kim, W.K. and Netz, R.R. (2015). Barrier-induced dielectric counterion relaxation at super-low frequencies in salt-free polyelectrolyte solutions. Eur Phys J E, 38, 11: 15 doi: http://dx.doi.org/10.1140/epje/i2015-15120-6
Kim, W.K. and Netz, R.R. (2015). The mean shape of transition and first-passage paths. J Chem Phys, 143, 22: 15 doi: http://dx.doi.org/10.1063/1.4936408
Klauss, A., Haumann, M. and Dau, H. (2015). Seven Steps of Alternating Electron and Proton Transfer in Photosystem II Water Oxidation Traced by Time-Resolved Photothermal Beam Deflection at Improved Sensitivity. J Phys Chem B, 119, 6: 2677-2689 doi: http://dx.doi.org/10.1021/jp509069p
Kuhne, J., Eisenhauer, K., Ritter, E., Hegemann, P., Gerwert, K. and Bartl, F. (2015). Early formation of the ion-conducting pore in channelrhodopsin-2. Angew Chem Int Ed Engl, 54, 16: 4953-4957 doi: http://dx.doi.org/10.1002/anie.201410180
Lorch, S., Capponi, S., Pieront, F. and Bondar, A.N. (2015). Dynamic Carboxylate/Water Networks on the Surface of the PsbO Subunit of Photosystem II. J Phys Chem B, 119, 37: 12172-12181 doi: http://dx.doi.org/10.1021/acs.jpcb.5b06594
Lórenz-Fonfría, V.A., Bamann, C., Resler, T., Schlesinger, R., Bamberg, E. and Heberle, J. (2015). Temporal evolution of helix hydration in a light-gated ion channel correlates with ion conductance. Proc Natl Acad Sci U S A, 112, 43: E5796-E5804 doi: http://dx.doi.org/10.1073/pnas.1511462112
Lórenz-Fonfría, V.A., Schultz, B.J., Resler, T., Schlesinger, R., Bamann, C., Bamberg, E. and Heberle, J. (2015). Pre-Gating Conformational Changes in the ChETA Variant of Channelrhodopsin-2 Monitored by Nanosecond IR Spectroscopy. J Am Chem Soc, 137, 5: 1850-1861 doi: http://dx.doi.org/10.1021/ja5108595
Luck, M., Bruun, S., Keidel, A., Hegemann, P. and Hildebrandt, P. (2015). Photochemical chromophore isomerization in histidine kinase rhodopsin HKR1. Febs Letters, 589, 10: 1067-1071 doi: http://dx.doi.org/10.1016/j.febslet.2015.03.024
Ly, H.K., Wrzolek, P., Heidary, N., Gotz, R., Horch, M., Kozuch, J., Schwalbe, M. and Weidinger, I.M. (2015). 2(nd) coordination sphere controlled electron transfer of iron hangman complexes on electrodes probed by surface enhanced vibrational spectroscopy. Chem Sci, 6, 12: 6999-7007 doi: http://dx.doi.org/10.1039/c5sc02560e
Mattioli, G., Zaharieva, I., Dau, H. and Guidoni, L. (2015). Atomistic Texture of Amorphous Manganese Oxides for Electrochemical Water Splitting Revealed by Ab Initio Calculations Combined with X-ray Spectroscopy. J Am Chem Soc, 137, 32: 10254-10267 doi: http://dx.doi.org/10.1021/jacs.5b05174
Meyer, T. and Knapp, E.W. (2015). pKa values in proteins determined by electrostatics applied to molecular dynamics trajectories. J Chem Theory Comput, 11, 6: 2827-2840 doi: http://dx.doi.org/10.1021/acs.jctc.5b00123
Muh, F., DiFiore, D. and Zouni, A. (2015). The influence of poly(ethylene glycol) on the micelle formation of alkyl maltosides used in membrane protein crystallization. Phys Chem Chem Phys, 17, 17: 11678-11691 doi: http://dx.doi.org/10.1039/c5cp00431d
Pyta, K., Przybylski, P. and Bartl, F. (2015). Regioselective Long-Range Proton Transfer in New Rifamycin Antibiotics: A Process in which Crown Ethers Act as Stronger Br⊘nsted Bases than Amines. ChemPhysChem, 16, 5: 938-942 doi: http://dx.doi.org/10.1002/cphc.201402892
Resler, T., Schultz, B.J., Lórenz-Fonfría, V.A., Schlesinger, R. and Heberle, J. (2015). Kinetic and Vibrational Isotope Effects of Proton Transfer Reactions in Channelrhodopsin-2. Biophys J, 109, 2: 287-297 doi: http://dx.doi.org/10.1016/j.bpj.2015.06.023
Richter, C., Schneider, C., Quick, M.T., Volz, P., Mahrwald, R., Hughes, J., Dick, B., Alexiev, U. and Ernsting, N.P. (2015). Dual-fluorescence pH probe for bio-labelling. Phys Chem Chem Phys, 17, 45: 30590-30597 doi: http://dx.doi.org/10.1039/c5cp05454k
Richter, F., Scheib, U.S., Mehlhorn, J., Schubert, R., Wietek, J., Gernetzki, O., Hegemann, P., Mathes, T. and Moglich, A. (2015). Upgrading a microplate reader for photobiology and all-optical experiments. Photochem Photobiol Sci, 14, 2: 270-279 doi: http://dx.doi.org/10.1039/c4pp00361f
Rinne, K.F., Schulz, J.C.F. and Netz, R.R. (2015). Impact of secondary structure and hydration water on the dielectric spectrum of poly-alanine and possible relation to the debate on slaved versus slaving water. J Chem Phys, 142, 21: 13 doi: http://dx.doi.org/10.1063/1.4921777
Rose, A.S., Zachariae, U., Grubmüller, H., Hofmann, K.P., Scheerer, P. and Hildebrand, P.W. (2015). Role of Structural Dynamics at the Receptor G Protein Interface for Signal Transduction. Plos One, 10, 11: 13 doi: http://dx.doi.org/10.1371/journal.pone.0143399
Rost, B.R., Schneider, F., Grauel, M.K., Wozny, C., Bentz, C.G., Blessing, A., Rosenmund, T., Jentsch, T.J., Schmitz, D., Hegemann, P. and Rosenmund, C. (2015). Optogenetic acidification of synaptic vesicles and lysosomes. Nat Neurosci, 18, 12: 1845-1852 doi: http://dx.doi.org/10.1038/nn.4161
Sakalli, I. and Knapp, E.W. (2015). pK_A in Proteins Solving the Poisson-Boltzmann Equation with Finite Elements. J Comput Chem, 36, 29: 2147-2157 doi: http://dx.doi.org/10.1002/jcc.24053
Scheerer, P., Zhang, F., Kalms, J., von Stetten, D., Krauss, N., Oberpichler, I. and Lamparter, T. (2015). The class III cyclobutane pyrimidine dimer photolyase structure reveals a new antenna chromophore binding site and alternative photoreduction pathways. J Biol Chem, 290, 18: 11504-11514 doi: http://dx.doi.org/10.1074/jbc.M115.637868
Scheib, U., Stehfest, K., Gee, C.E., Körschen, H.G., Fudim, R., Oertner, T.G. and Hegemann, P. (2015). The rhodopsin-guanylyl cyclase of the aquatic fungus Blastocladiella emersonii enables fast optical control of cGMP signaling. Sci Signal, 8, 389: 8 doi: http://dx.doi.org/10.1126/scisignal.aab0611
Schneider, F., Grimm, C. and Hegemann, P. (2015). Biophysics of Channelrhodopsin. Annu Rev Biophys, 44, 167-186 doi: http://dx.doi.org/10.1146/annurev-biophys-060414-034014
Schwierz, N., Horinek, D. and Netz, R.R. (2015). Specific Ion Binding to Carboxylic Surface Groups and the pH Dependence of the Hofmeister Series. Langmuir, 31, 1: 215-225 doi: http://dx.doi.org/10.1021/la503813d
Sezer, M., Kielb, P., Kuhlmann, U., Mohrmann, H., Schulz, C., Heinrich, D., Schlesinger, R., Heberle, J. and Weidinger, I.M. (2015). Surface Enhanced Resonance Raman Spectroscopy Reveals Potential Induced Redox and Conformational Changes of Cytochrome c Oxidase on Electrodes. J Phys Chem B, 119, 30: 9586-9591 doi: http://dx.doi.org/10.1021/acs.jpcb.5b03206
Skandary, S., Hussels, M., Konrad, A., Renger, T., Müh, F., Bommer, M., Zouni, A., Meixner, A.J. and Brecht, M. (2015). Variation of Exciton-Vibrational Coupling in Photosystem II Core Complexes from Thermosynechococcus elongatus As Revealed by Single-Molecule Spectroscopy. J Phys Chem B, 119, 11: 4203-4210 doi: http://dx.doi.org/10.1021/jp510631x
Song, C., Escobar, F.V., Xu, X.L., Narikawa, R., Ikeuchi, M., Siebert, F., Gärtner, W., Matysik, J. and Hildebrandt, P. (2015). A Red/Green Cyanobacteriochrome Sustains Its Color Despite a Change in the Bilin Chromophore's Protonation State. Biochemistry, 54, 38: 5839-5848 doi: http://dx.doi.org/10.1021/acs.biochem.5b00735
Stensitzki, T., Muders, V., Schlesinger, R., Heberle, J. and Heyne, K. (2015). The primary photoreaction of channelrhodopsin-1: wavelength dependent photoreactions induced by ground-state heterogeneity. Front Mol Biosci, 2, 41 doi: http://dx.doi.org/10.3389/fmolb.2015.00041
Vogt, A., Guo, Y., Tsunoda, S.P., Kateriya, S., Elstner, M. and Hegemann, P. (2015). Conversion of a light-driven proton pump into a light-gated ion channel. Sci Rep, 5, 13 doi: http://dx.doi.org/10.1038/srep16450
Volz, P., Boreham, A., Wolf, A., Kim, T.Y., Balke, J., Frombach, J., Hadam, S., Afraz, Z., Rancan, F., Blume-Peytavi, U., Vogt, A. and Alexiev, U. (2015). Application of Single Molecule Fluorescence Microscopy to Characterize the Penetration of a Large Amphiphilic Molecule in the Stratum Corneum of Human Skin. Int J Mol Sci, 16, 4: 6960-6977 doi: http://dx.doi.org/10.3390/ijms16046960
Weidinger, I.M. (2015). Analysis of structure-function relationships in cytochrome c oxidase and its biomimetic analogs via resonance Raman and surface enhanced resonance Raman spectroscopies. Biochim Biophys Acta, 1847, 1: 119-125 doi: http://dx.doi.org/10.1016/j.bbabio.2014.09.002
Wietek, J., Beltramo, R., Scanziani, M., Hegemann, P., Oertner, T.G. and Wiegert, J.S. (2015). An improved chloride-conducting channelrhodopsin for light-induced inhibition of neuronal activity in vivo. Sci Rep, 5, 11 doi: http://dx.doi.org/10.1038/srep14807
Zhang, C., Chen, C., Dong, H., Shen, J.R., Dau, H. and Zhao, J. (2015). Inorganic chemistry. A synthetic Mn(4)Ca-cluster mimicking the oxygen-evolving center of photosynthesis. Science, 348, 6235: 690-693 doi: http://dx.doi.org/10.1126/science.aaa6550

2016 back up ↑

Alonso-Mori, R., Asa, K., Bergmann, U., Brewster, A.S., Chatterjee, R., Cooper, J.K., Frei, H.M., Fuller, F.D., Goggins, E., Gul, S., Fukuzawa, H., Iablonskyi, D., Ibrahim, M., Katayama, T., Kroll, T., Kumagai, Y., McClure, B.A., Messinger, J., Motomura, K., Nagaya, K., Nishiyama, T., Saracini, C., Sato, Y., Sauter, N.K., Sokaras, D., Takanashi, T., Togashi, T., Ueda, K., Weare, W.W., Weng, T.C., Yabashi, M., Yachandra, V.K., Young, I.D., Zouni, A., Kern, J.F. and Yano, J. (2016). Towards characterization of photo-excited electron transfer and catalysis in natural and artificial systems using XFELs. Faraday Discuss, 194, 621-638 doi: http://dx.doi.org/10.1039/c6fd00084c
Banthiya, S., Kalms, J., Yoga, E.G., Ivanov, I., Carpena, X., Hamberg, M., Kuhn, H. and Scheerer, P. (2016). Structural and functional basis of phospholipid oxygenase activity of bacterial lipoxygenase from Pseudomonas aeruginosa. Biochim Biophys Acta Mol Cell Biol Lipids, 1861, 11: 1681-1692 doi: http://dx.doi.org/10.1016/j.bbalip.2016.08.002
Baxter, E.L., Aguila, L., Alonso-Mori, R., Barnes, C.O., Bonagura, C.A., Brehmer, W., Brunger, A.T., Calero, G., Caradoc-Davies, T.T., Chatterjee, R., Degrado, W.F., Fraser, J.S., Ibrahim, M., Kern, J., Kobilka, B.K., Kruse, A.C., Larsson, K.M., Lemke, H.T., Lyubimov, A.Y., Manglik, A., McPhillips, S.E., Norgren, E., Pang, S.S., Soltis, S.M., Song, J.H., Thomaston, J., Tsai, Y., Weis, W.I., Woldeyes, R.A., Yachandra, V., Yano, J., Zouni, A. and Cohen, A.E. (2016). High-density grids for efficient data collection from multiple crystals. Acta Crystallogr Sect D-Struct Biol, 72, 2-11 doi: http://dx.doi.org/10.1107/s2059798315020847
Berndt, A., Lee, S.Y., Wietek, J., Ramakrishnan, C., Steinberg, E.E., Rashid, A.J., Kim, H., Park, S., Santoro, A., Frankland, P.W., Iyer, S.M., Pak, S., Ährlund-Richter, S., Delp, S.L., Malenka, R.C., Josselyn, S.A., Carlen, M., Hegemann, P. and Deisseroth, K. (2016). Structural foundations of optogenetics: Determinants of channelrhodopsin ion selectivity. Proc Natl Acad Sci U S A, 113, 4: 822-829 doi: http://dx.doi.org/10.1073/pnas.1523341113
Block, S., Zhdanov, V.P. and Hook, F. (2016). Quantification of Multivalent Interactions by Tracking Single Biological Nanoparticle Mobility on a Lipid Membrane. Nano Lett, 16, 7: 4382-4390 doi: http://dx.doi.org/10.1021/acs.nanolett.6b01511
Bommer, M., Bondar, A.N., Zouni, A., Dobbek, H. and Dau, H. (2016). Crystallographic and Computational Analysis of the Barrel Part of the PsbO Protein of Photosystem II: Carboxylate-Water Clusters as Putative Proton Transfer Relays and Structural Switches. Biochemistry, 55, 33: 4626-4635 doi: http://dx.doi.org/10.1021/acs.biochem.6b00441
Bonthuis, D.J., Mamatkulov, S.I. and Netz, R.R. (2016). Optimization of classical nonpolarizable force fields for OH^- and H₃O⁺. J Chem Phys, 144, 10: 10 doi: http://dx.doi.org/10.1063/1.4942771
Bonthuis, D.J., Uematsu, Y. and Netz, R.R. (2016). Interfacial layer effects on surface capacitances and electro-osmosis in electrolytes. Philos Trans R Soc A-Math Phys Eng Sci, 374, 2060: 9 doi: http://dx.doi.org/10.1098/rsta.2015.0033
Buhrke, D., Escobar, F.V., Sauthof, L., Wilkening, S., Herder, N., Tavraz, N.N., Willoweit, M., Keidel, A., Utesch, T., Mroginski, M.A., Schmitt, F.J., Hildebrandt, P. and Friedrich, T. (2016). The role of local and remote amino acid substitutions for optimizing fluorescence in bacteriophytochromes: A case study on iRFP. Sci Rep, 6, 12 doi: http://dx.doi.org/10.1038/srep28444
Chernev, P., Zaharieva, I., Rossini, E., Galstyan, A., Dau, H. and Knapp, E.W. (2016). Merging Structural Information from X-ray Crystallography, Quantum Chemistry, and EXAFS Spectra: The Oxygen-Evolving Complex in PSII. J Phys Chem B, 120, 42: 10899-10922 doi: http://dx.doi.org/10.1021/acs.jpcb.6b05800
Daldrop, J.O., Kim, W.K. and Netz, R.R. (2016). Transition paths are hot. Epl, 113, 1: 6 doi: http://dx.doi.org/10.1209/0295-5075/113/18004
Damrow, R., Maldener, I. and Zilliges, Y. (2016). The Multiple Functions of Common Microbial Carbon Polymers, Glycogen and PHB, during Stress Responses in the Non-Diazotrophic Cyanobacterium Synechocystis sp. PCC 6803. Front Microbiol, 7, 966 doi: http://dx.doi.org/10.3389/fmicb.2016.00966
Gerecke, M., Bierhance, G., Gutmann, M., Ernsting, N.P. and Rosspeintner, A. (2016). Femtosecond broadband fluorescence upconversion spectroscopy: Spectral coverage versus efficiency. Rev Sci Instrum, 87, 5: 053115 doi: http://dx.doi.org/10.1063/1.4948932
González-Flores, D., Zaharieva, I., Heidkamp, J., Chernev, P., Martínez-Moreno, E., Pasquini, C., Mohammadi, M.R., Klingan, K., Gernet, U., Fischer, A. and Dau, H. (2016). Electrosynthesis of Biomimetic Manganese-Calcium Oxides for Water Oxidation CatalysisAtomic Structure and Functionality. ChemSusChem, 9, 4: 379-387 doi: http://dx.doi.org/10.1002/cssc.201501399
Jagtap, A.P., Geiger, M.A., Stöppler, D., Orwick-Rydmark, M., Oschkinat, H. and Sigurdsson, S.T. (2016). bcTol: a highly water-soluble biradical for efficient dynamic nuclear polarization of biomolecules. Chem Commun, 52, 43: 7020-7023 doi: http://dx.doi.org/10.1039/c6cc01813k
Kalms, J., Schmidt, A., Frielingsdorf, S., van der Linden, P., von Stetten, D., Lenz, O., Carpentier, P. and Scheerer, P. (2016). Krypton Derivatization of an O₂-Tolerant Membrane-Bound NiFe Hydrogenase Reveals a Hydrophobic Tunnel Network for Gas Transport. Angew Chem-Int Edit, 55, 18: 5586-5590 doi: http://dx.doi.org/10.1002/anie.201508976
Mohrmann, H., Kube, I., Lorenz-Fonfria, V.A., Engelhard, M. and Heberle, J. (2016). Transient Conformational Changes of Sensory Rhodopsin II Investigated by Vibrational Stark Effect Probes. J Phys Chem B, 120, 19: 4383-4387 doi: http://dx.doi.org/10.1021/acs.jpcb.6b01900
Nagano, S., Scheerer, P., Zubow, K., Michael, N., Inomata, K., Lamparter, T. and Krauss, N. (2016). The Crystal Structures of the N-terminal Photosensory Core Module of Agrobacterium Phytochrome Agp1 as Parallel and Anti-parallel Dimers. J Biol Chem, 291, 39: 20674-20691 doi: http://dx.doi.org/10.1074/jbc.M116.739136
Nango, E., Royant, A., Kubo, M., Nakane, T., Wickstrand, C., Kimura, T., Tanaka, T., Tono, K., Song, C.Y., Tanaka, R., Arima, T., Yamashita, A., Kobayashi, J., Hosaka, T., Mizohata, E., Nogly, P., Sugahara, M., Nam, D., Nomura, T., Shimamura, T., Im, D., Fujiwara, T., Yamanaka, Y., Jeon, B., Nishizawa, T., Oda, K., Fukuda, M., Andersson, R., Båth, P., Dods, R., Davidsson, J., Matsuoka, S., Kawatake, S., Murata, M., Nureki, O., Owada, S., Kameshima, T., Hatsui, T., Joti, Y., Schertler, G., Yabashi, M., Bondar, A.N., Standfuss, J., Neutze, R. and Iwata, S. (2016). A three-dimensional movie of structural changes in bacteriorhodopsin. Science, 354, 6319: 1552-1557 doi: http://dx.doi.org/10.1126/science.aah3497
Otero, L.H., Klinke, S., Rinaldi, J., Velázquez-Escobar, F., Mroginski, M.A., López, M.F., Malamud, F., Vojnov, A.A., Hildebrandt, P., Goldbaum, F.A. and Bonomi, H.R. (2016). Structure of the Full-Length Bacteriophytochrome from the Plant Pathogen Xanthomonas campestris Provides Clues to its Long-Range Signaling Mechanism. J Mol Biol, 428, 19: 3702-3720 doi: http://dx.doi.org/10.1016/j.jmb.2016.04.012
Reidelbach, M., Betz, F., Mäusle, R.M. and Imhof, P. (2016). Proton transfer pathways in an aspartate-water cluster sampled by a network of discrete states. Chem Phys Lett, 659, 169-175 doi: http://dx.doi.org/10.1016/j.cplett.2016.07.021
Richter, C., Ernsting, N.P. and Mahrwald, R. (2016). Operationally Simple and Selective One-Pot Synthesis of Hydroxyphenones: A Facile Access to SNARF Dyes. Synthesis, 48, 8: 1217-1225 doi: http://dx.doi.org/10.1055/s-0035-1561370
Roessler, C.G., Agarwal, R., Allaire, M., Alonso-Mori, R., Andi, B., Bachega, J.F.R., Bommer, M., Brewster, A.S., Browne, M.C., Chatterjee, R., Cho, E., Cohen, A.E., Cowan, M., Datwani, S., Davidson, V.L., Defever, J., Eaton, B., Ellson, R., Feng, Y.P., Ghislain, L.P., Glownia, J.M., Han, G.Y., Hattne, J., Hellmich, J., Heroux, A., Ibrahim, M., Kern, J., Kuczewski, A., Lemke, H.T., Liu, P.H., Majlof, L., McClintock, W.M., Myers, S., Nelsen, S., Olechno, J., Orville, A.M., Sauter, N.K., Soares, A.S., Soltis, S.M., Song, H., Stearns, R.G., Tran, R., Tsai, Y., Uervirojnangkoorn, M., Wilmot, C.M., Yachandra, V., Yano, J., Yukl, E.T., Zhu, D.L. and Zouni, A. (2016). Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography. Structure, 24, 4: 631-640 doi: http://dx.doi.org/10.1016/j.str.2016.02.007
Rossini, E. and Knapp, E.W. (2016). Proton solvation in protic and aprotic solvents. J Comput Chem, 37, 12: 1082-1091 doi: http://dx.doi.org/10.1002/jcc.24297
Rossini, E., Netz, R.R. and Knapp, E.W. (2016). Computing pKa Values in Different Solvents by Electrostatic Transformation. J Chem Theory Comput, 12, 7: 3360-3369 doi: http://dx.doi.org/10.1021/acs.jctc.6b00446
Schlaich, A., Knapp, E.W. and Netz, R.R. (2016). Water Dielectric Effects in Planar Confinement. Physical Review Letters, 117, 4: 5 doi: http://dx.doi.org/10.1103/PhysRevLett.117.048001
Schnedermann, C., Muders, V., Ehrenberg, D., Schlesinger, R., Kukura, P. and Heberle, J. (2016). Vibronic Dynamics of the Ultrafast all-trans to 13-cis Photoisomerization of Retinal in Channelrhodopsin-1. J Am Chem Soc, 138, 14: 4757-4762 doi: http://dx.doi.org/10.1021/jacs.5b12251
Schreiner, M., Schlesinger, R., Heberle, J. and Niemann, H.H. (2016). Crystal structure of Halobacterium salinarum halorhodopsin with a partially depopulated primary chloride-binding site. Acta Crystallogr F Struct Biol Commun, 72, Pt 9: 692-699 doi: http://dx.doi.org/10.1107/S2053230X16012796
Schwierz, N., Horinek, D., Sivan, U. and Netz, R.R. (2016). Reversed Hofmeister series-The rule rather than the exception. Curr Opin Colloid Interface Sci, 23, 10-18 doi: http://dx.doi.org/10.1016/j.cocis.2016.04.003
Sierra, R.G., Gati, C., Laksmono, H., Dao, E.H., Gul, S., Fuller, F., Kern, J., Chatterjee, R., Ibrahim, M., Brewster, A.S., Young, I.D., Michels-Clark, T., Aquila, A., Liang, M., Hunter, M.S., Koglin, J.E., Boutet, S., Junco, E.A., Hayes, B., Bogan, M.J., Hampton, C.Y., Puglisi, E.V., Sauter, N.K., Stan, C.A., Zouni, A., Yano, J., Yachandra, V.K., Soltis, S.M., Puglisi, J.D. and DeMirci, H. (2016). Concentric-flow electrokinetic injector enables serial crystallography of ribosome and photosystem II. Nat Methods, 13, 1: 59-+ doi: http://dx.doi.org/10.1038/nmeth.3667
Sprink, T., Ramrath, D.J.F., Yamamoto, H., Yamamoto, K., Loerke, J., Ismer, J., Hildebrand, P.W., Scheerer, P., Bürger, J., Mielke, T. and Spahn, C.M.T. (2016). Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association. Sci Adv, 2, 3: 6 doi: http://dx.doi.org/10.1126/sciadv.1501502
Stensitzki, T., Yang, Y., Berg, A., Mahammed, A., Gross, Z. and Heyne, K. (2016). Ultrafast electronic and vibrational dynamics in brominated aluminum corroles: Energy relaxation and triplet formation. Struct Dyn, 3, 4: 043210 doi: http://dx.doi.org/10.1063/1.4949363
Stensitzki, T., Yang, Y., Muders, V., Schlesinger, R., Heberle, J. and Heyne, K. (2016). Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization. Struct Dyn, 3, 4: 043208 doi: http://dx.doi.org/10.1063/1.4948338
Stöppler, D., Song, C., van Rossum, B.J., Geiger, M.A., Lang, C., Mroginski, M.A., Jagtap, A.P., Sigurdsson, S.T., Matysik, J., Hughes, J. and Oschkinat, H. (2016). Dynamic Nuclear Polarization Provides New Insights into Chromophore Structure in Phytochrome Photoreceptors. Angew Chem-Int Edit, 55, 52: 16017-16020 doi: http://dx.doi.org/10.1002/anie.201608119
Süss, B., Ringleb, F. and Heberle, J. (2016). New ultrarapid-scanning interferometer for FT-IR spectroscopy with microsecond time-resolution. Rev Sci Instrum, 87, 6: 7 doi: http://dx.doi.org/10.1063/1.4953658
Volz, P., Krause, N., Balke, J., Schneider, C., Walter, M., Schneider, F., Schlesinger, R. and Alexiev, U. (2016). Light and pH-induced Changes in Structure and Accessibility of Transmembrane Helix B and Its Immediate Environment in Channelrhodopsin-2. J Biol Chem, 291, 33: 17382-17393 doi: http://dx.doi.org/10.1074/jbc.M115.711200
Wietek, J., Broser, M., Krause, B.S. and Hegemann, P. (2016). Identification of a Natural Green Light Absorbing Chloride Conducting Channelrhodopsin from Proteomonas sulcata. J Biol Chem, 291, 8: 4121-4127 doi: http://dx.doi.org/10.1074/jbc.M115.699637
Wolf, A., Schneider, C., Kim, T.Y., Kirchberg, K., Volz, P. and Alexiev, U. (2016). A simulation-guided fluorescence correlation spectroscopy tool to investigate the protonation dynamics of cytochrome c oxidase. Phys Chem Chem Phys, 18, 18: 12877-12885 doi: http://dx.doi.org/10.1039/c5cp07925j
Yang, Y., Heyne, K., Mathies, R.A. and Dasgupta, J. (2016). Non-Bonded Interactions Drive the Sub-Picosecond Bilin Photoisomerization in the P_fr State of Phytochrome Cph1. ChemPhysChem, 17, 3: 369-374 doi: http://dx.doi.org/10.1002/cphc.201501073
Young, I.D., Ibrahim, M., Chatterjee, R., Gul, S., Fuller, F.D., Koroidov, S., Brewster, A.S., Tran, R., Alonso-Mori, R., Kroll, T., Michels-Clark, T., Laksmono, H., Sierra, R.G., Stan, C.A., Hussein, R., Zhang, M., Douthit, L., Kubin, M., de Lichtenberg, C., Pham, L.V., Nilsson, H., Cheah, M.H., Shevela, D., Saracini, C., Bean, M.A., Seuffert, I., Sokaras, D., Weng, T.C., Pastor, E., Weninger, C., Fransson, T., Lassalle, L., Bräuer, P., Aller, P., Docker, P.T., Andi, B., Orville, A.M., Glownia, J.M., Nelson, S., Sikorski, M., Zhu, D.L., Hunter, M.S., Lane, T.J., Aquila, A., Koglin, J.E., Robinson, J., Liang, M.N., Boutet, S., Lyubimov, A.Y., Uervirojnangkoorn, M., Moriarty, N.W., Liebschner, D., Afonine, P.V., Waterman, D.G., Evans, G., Wernet, P., Dobbek, H., Weis, W.I., Brunger, A.T., Zwart, P.H., Adams, P.D., Zouni, A., Messinger, J., Bergmann, U., Sauter, N.K., Kern, J., Yachandra, V.K. and Yano, J. (2016). Structure of photosystem II and substrate binding at room temperature. Nature, 540, 7633: 453-+ doi: http://dx.doi.org/10.1038/nature20161
Zaharieva, I., Chernev, P., Berggren, G., Anderlund, M., Styring, S., Dau, H. and Haumann, M. (2016). Room-Temperature Energy-Sampling Kβ X-ray Emission Spectroscopy of the Mn₄Ca Complex of Photosynthesis Reveals Three Manganese-Centered Oxidation Steps and Suggests a Coordination Change Prior to O₂ Formation. Biochemistry, 55, 30: 4197-4211 doi: http://dx.doi.org/10.1021/acs.biochem.6b00491
Zaharieva, I., Dau, H. and Haumann, M. (2016). Sequential and Coupled Proton and Electron Transfer Events in the S₂ → S₃ Transition of Photosynthetic Water Oxidation Revealed by Time-Resolved X-ray Absorption Spectroscopy. Biochemistry, 55, 50: 6996-7004 doi: http://dx.doi.org/10.1021/acs.biochem.6b01078
Zaharieva, I., González-Flores, D., Asfari, B., Pasquini, C., Mohammadi, M.R., Klingan, K., Zizak, I., Loos, S., Chernev, P. and Dau, H. (2016). Water oxidation catalysis - role of redox and structural dynamics in biological photosynthesis and inorganic manganese oxides. Energy Environ Sci, 9, 7: 2433-2443 doi: http://dx.doi.org/10.1039/c6ee01222a
Zilliges, Y. and Dau, H. (2016). Unexpected capacity for organic carbon assimilation by Thermosynechococcus elongatus, a crucial photosynthetic model organism. Febs Letters, 590, 7: 962-970 doi: http://dx.doi.org/10.1002/1873-3468.12120

2017 back up ↑

Berg, J., Block, S., Höök, F. and Brzezinski, P. (2017). Single Proteoliposomes with E. coli Quinol Oxidase: Proton Pumping without Transmembrane Leaks. Israel Journal of Chemistry, 57, 5: 437-445 doi: http://dx.doi.org/10.1002/ijch.201600138
Bommer, M., Coates, L., Dau, H., Zouni, A. and Dobbek, H. (2017). Protein crystallization and initial neutron diffraction studies of the photosystem II subunit PsbO. Acta Crystallogr F-Struct Biol Commun, 73, 525-531 doi: http://dx.doi.org/10.1107/s2053230x17012171
Bondar, A.N. and Smith, J.C. (2017). Protonation-state-Coupled Conformational Dynamics in Reaction Mechanisms of Channel and Pump Rhodopsins. Photochem Photobiol Sci, 93, 6: 1336-1344 doi: http://dx.doi.org/10.1111/php.12790
del Val, C. and Bondar, A.N. (2017). Charged groups at binding interfaces of the PsbO subunit of photosystem II: A combined bioinformatics and simulation study. Biochim Biophys Acta Bioenerg, 1858, 6: 432-441 doi: http://dx.doi.org/10.1016/j.bbabio.2017.03.004
Escobar, F.V., Buhrke, D., Fernandez Lopez, M., Shenkutie, S.M., von Horsten, S., Essen, L.O., Hughes, J. and Hildebrandt, P. (2017). Structural communication between the chromophore-binding pocket and the N-terminal extension in plant phytochrome phyB. FEBS Lett, 591, 9: 1258-1265 doi: http://dx.doi.org/10.1002/1873-3468.12642
Escobar, F.V., Buhrke, D., Michael, N., Sauthof, L., Wilkening, S., Tavraz, N.N., Salewski, J., Frankenberg-Dinkel, N., Mroginski, M.A., Scheerer, P., Friedrich, T., Siebert, F. and Hildebrandt, P. (2017). Common Structural Elements in the Chromophore Binding Pocket of the Pfr State of Bathy Phytochromes. Photochem Photobiol, 93, 3: 724-732 doi: http://dx.doi.org/10.1111/php.12742
Escobar, F.V., Lang, C., Takiden, A., Schneider, C., Balke, J., Hughes, J., Alexiev, U., Hildebrandt, P. and Mroginski, M.A. (2017). Protonation-Dependent Structural Heterogeneity in the Chromophore Binding Site of Cyanobacterial Phytochrome Cph1. J Phys Chem B, 121, 1: 47-57 doi: http://dx.doi.org/10.1021/acs.jpcb.6b09600
Friedrich, R., Block, S., Alizadehheidari, M., Heider, S., Fritzsche, J., Esbjorner, E.K., Westerlund, F. and Bally, M. (2017). A nano flow cytometer for single lipid vesicle analysis. Lab Chip, 17, 5: 830-841 doi: http://dx.doi.org/10.1039/c6lc01302c
Fuller, F.D., Gul, S., Chatterjee, R., Burgie, E.S., Young, I.D., Lebrette, H., Srinivas, V., Brewster, A.S., Michels-Clark, T., Clinger, J.A., Andi, B., Ibrahim, M., Pastor, E., de Lichtenberg, C., Hussein, R., Pollock, C.J., Zhang, M., Stan, C.A., Kroll, T., Fransson, T., Weninger, C., Kubin, M., Aller, P., Lassalle, L., Bräuer, P., Miller, M.D., Amin, M., Koroidov, S., Roessler, C.G., Allaire, M., Sierra, R.G., Docker, P.T., Glownia, J.M., Nelson, S., Koglin, J.E., Zhu, D.L., Chollet, M., Song, S., Lemke, H., Liang, M.N., Sokaras, D., Alonso-Mori, R., Zouni, A., Messinger, J., Bergmann, U., Boal, A.K., Bollinger, J.M., Krebs, C., Högbom, M., Phillips, G.N., Vierstra, R.D., Sauter, N.K., Orville, A.M., Kern, J., Yachandra, V.K. and Yano, J. (2017). Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers. Nat Methods, 14, 4: 443-+ doi: http://dx.doi.org/10.1038/nmeth.4195
Grimm, C., Vierock, J., Hegemann, P. and Wietek, J. (2017). Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins. J Vis Exp, 123: 8 doi: http://dx.doi.org/10.3791/55497
Guerra, F. and Bondar, A.N. (2017). Dynamic Hydrogen-Bonding Networks in Photosystem II. Biophys J, 112, 3: 507A-507A doi: http://dx.doi.org/10.1016/j.bpj.2016.11.2741
Harris, N.J., Reading, E., Ataka, K., Grzegorzewski, L., Charalambous, K., Liu, X., Schlesinger, R., Heberle, J. and Booth, P.J. (2017). Structure formation during translocon-unassisted co-translational membrane protein folding. Sci Rep, 7, 1: 8021 doi: http://dx.doi.org/10.1038/s41598-017-08522-9
Helabad, M.B., Ghane, T., Reidelbach, M., Woelke, A.L., Knapp, E.W. and Imhof, P. (2017). Protonation-State-Dependent Communication in Cytochrome c Oxidase. Biophys J, 113, 4: 817-828 doi: http://dx.doi.org/10.1016/j.bpj.2017.07.005
Hontani, Y., Broser, M., Silapetere, A., Krause, B.S., Hegemann, P. and Kennis, J.T.M. (2017). The femtosecond-to-second photochemistry of red-shifted fast-closing anion channelrhodopsin PsACR1. Phys Chem Chem Phys, 19, 45: 30402-30409 doi: http://dx.doi.org/10.1039/c7cp06414d
Hontani, Y., Marazzi, M., Stehfest, K., Mathes, T., van Stokkum, I.H.M., Elstner, M., Hegemann, P. and Kennis, J.T.M. (2017). Reaction dynamics of the chimeric channelrhodopsin C1C2. Sci Rep, 7, 12 doi: http://dx.doi.org/10.1038/s41598-017-07363-w
Kacprzak, S., Njimona, I., Renz, A., Feng, J., Reijerse, E., Lubitz, W., Krauss, N., Scheerer, P., Nagano, S., Lamparter, T. and Weber, S. (2017). Intersubunit distances in full-length, dimeric, bacterial phytochrome Agp1, as measured by pulsed electron-electron double resonance (PELDOR) between different spin label positions, remain unchanged upon photoconversion. J Biol Chem, 292, 18: 7598-7606 doi: http://dx.doi.org/10.1074/jbc.M116.761882
Kalms, J., Banthiya, S., Yoga, E.G., Hamberg, M., Holzhutter, H.G., Kuhn, H. and Scheerer, P. (2017). The crystal structure of Pseudomonas aeruginosa lipoxygenase Ala420Gly mutant explains the improved oxygen affinity and the altered reaction specificity. Biochim Biophys Acta Mol Cell Biol Lipids, 1862, 5: 463-473 doi: http://dx.doi.org/10.1016/j.bbalip.2017.01.003
Kaufmann, J.C.D., Krause, B.S., Grimm, C., Ritter, E., Hegemann, P. and Bartl, F.J. (2017). Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function. J Biol Chem, 292, 34: 14205-14216 doi: http://dx.doi.org/10.1074/jbc.M117.779629
Kielb, P., Utesch, T., Kozuch, J., Jeoung, J.H., Dobbek, H., Mroginski, M.A., Hildebrandt, P. and Weidinger, I. (2017). Switchable Redox Chemistry of the Hexameric Tyrosine-Coordinated Heme Protein. J Phys Chem B, 121, 16: 3955-3964 doi: http://dx.doi.org/10.1021/acs.jpcb.7b01286
Kottke, T., Lorenz-Fonfria, V.A. and Heberle, J. (2017). The Grateful Infrared: Sequential Protein Structural Changes Resolved by Infrared Difference Spectroscopy. J Phys Chem B, 121, 2: 335-350 doi: http://dx.doi.org/10.1021/acs.jpcb.6b09222
Krause, B.S., Grimm, C., Kaufmann, J.C.D., Schneider, F., Sakmar, T.P., Bartl, F.J. and Hegemann, P. (2017). Complex Photochemistry within the Green-Absorbing Channelrhodopsin ReaChR. Biophys J, 112, 6: 1166-1175 doi: http://dx.doi.org/10.1016/j.bpj.2017.02.001
Lamparter, T., Krauss, N. and Scheerer, P. (2017). Phytochromes from Agrobacterium fabrum. Photochem Photobiol Sci, 93, 3: 642-655 doi: http://dx.doi.org/10.1111/php.12761
Lorenz-Fonfria, V.A., Saita, M., Lazarova, T., Schlesinger, R. and Heberle, J. (2017). pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin. Proc Natl Acad Sci U S A, 114, 51: E10909-E10918 doi: http://dx.doi.org/10.1073/pnas.1707993114
Mamatkulov, S.I., Allolio, C., Netz, R.R. and Bonthuis, D.J. (2017). Orientation-Induced Adsorption of Hydrated Protons at the Air-Water Interface. Angew Chem-Int Edit, 56, 50: 15846-15851 doi: http://dx.doi.org/10.1002/anie.201707391
Mohrmann, H. and Heberle, J. (2017). Reply to "Comment on 'Transient Conformational Changes of Sensory Rhodopsin II Investigated by Vibrational Stark Effect Probes'". J Phys Chem B, 121, 30: 7397-7399 doi: http://dx.doi.org/10.1021/acs.jpcb.7b03453
Oberthuer, D., Knoska, J., Wiedorn, M.O., Beyerlein, K.R., Bushnell, D.A., Kovaleva, E.G., Heymann, M., Gumprecht, L., Kirian, R.A., Barty, A., Mariani, V., Tolstikova, A., Adriano, L., Awel, S., Barthelmess, M., Dörner, K., Xavier, P.L., Yefanov, O., James, D.R., Nelson, G., Wang, D.J., Calvey, G., Chen, Y.J., Schmidt, A., Szczepek, M., Frielingsdorf, S., Lenz, O., Snell, E., Robinson, P.J., Sarler, B., Belsak, G., Macek, M., Wilde, F., Aquila, A., Boutet, S., Liang, M.N., Hunter, M.S., Scheerer, P., Lipscomb, J.D., Weierstall, U., Kornberg, R.D., Spence, J.C.H., Pollack, L., Chapman, H.N. and Bajt, S. (2017). Double-flow focused liquid injector for efficient serial femtosecond crystallography. Sci Rep, 7, 10 doi: http://dx.doi.org/10.1038/srep44628
Rossini, E. and Knapp, E.-W. (2017). Protonation equilibria of transition metal complexes: From model systems toward the Mn-complex in photosystem II. Coordination Chemistry Reviews, 345, 16-30 doi: http://dx.doi.org/10.1016/j.ccr.2017.02.017
Rost, B.R., Schneider-Warme, F., Schmitz, D. and Hegemann, P. (2017). Optogenetic Tools for Subcellular Applications in Neuroscience. Neuron, 96, 3: 572-603 doi: http://dx.doi.org/10.1016/j.neuron.2017.09.047
Schuth, N., Liang, Z., Schonborn, M., Kussicke, A., Assuncao, R., Zaharieva, I., Zilliges, Y. and Dau, H. (2017). Inhibitory and Non-Inhibitory NH(3) Binding at the Water-Oxidizing Manganese Complex of Photosystem II Suggests Possible Sites and a Rearrangement Mode of Substrate Water Molecules. Biochemistry, 56, 47: 6240-6256 doi: http://dx.doi.org/10.1021/acs.biochem.7b00743
Sezer, M., Woelke, A.L., Knapp, E.W., Schlesinger, R., Mroginski, M.A. and Weidinger, I.M. (2017). Redox induced protonation of heme propionates in cytochrome c oxidase: Insights from surface enhanced resonance Raman spectroscopy and QM/MM calculations. Biochim Biophys Acta Bioenerg, 1858, 2: 103-108 doi: http://dx.doi.org/10.1016/j.bbabio.2016.10.009
Skandary, S., Müh, F., Ashraf, I., Ibrahim, M., Metzger, M., Zouni, A., Meixner, A.J. and Brecht, M. (2017). Role of missing carotenoid in reducing the fluorescence of single monomeric photosystem II core complexes. Phys Chem Chem Phys, 19, 20: 13189-13194 doi: http://dx.doi.org/10.1039/c6cp07748j
Stensitzki, T., Yang, Y., Wolke, A.L., Knapp, E.W., Hughes, J., Mroginski, M.A. and Heyne, K. (2017). Influence of Heterogeneity on the Ultrafast Photoisomerization Dynamics of Pfr in Cph1 Phytochrome. Photochem Photobiol, 93, 3: 703-712 doi: http://dx.doi.org/10.1111/php.12743
Takiden, A., Velazquez-Escobar, F., Dragelj, J., Woelke, A.L., Knapp, E.W., Piwowarski, P., Bart, F., Hildebrandt, P. and Mroginski, M.A. (2017). Structural and Vibrational Characterization of the Chromophore Binding Site of Bacterial Phytochrome Agp1. Photochem Photobiol Sci, 93, 3: 713-723 doi: http://dx.doi.org/10.1111/php.12737
Vierock, J., Grimm, C., Nitzan, N. and Hegemann, P. (2017). Molecular determinants of proton selectivity and gating in the red-light activated channelrhodopsin Chrimson. Sci Rep, 7, 15 doi: http://dx.doi.org/10.1038/s41598-017-09600-8
Wietek, J., Rodriguez-Rozada, S., Tutas, J., Tenedini, F., Grimm, C., Oertner, T.G., Soba, P., Hegemann, P. and Wiegert, J.S. (2017). Anion-conducting channelrhodopsins with tuned spectra and modified kinetics engineered for optogenetic manipulation of behavior. Sci Rep, 7, 18 doi: http://dx.doi.org/10.1038/s41598-017-14330-y
Zahn, C., Stensitzki, T., Gerecke, M., Berg, A., Mahammed, A., Gross, Z. and Heyne, K. (2017). Ultrafast Dynamics of Sb-Corroles: A Combined Vis-Pump Supercontinuum Probe and Broadband Fluorescence Up-Conversion Study. Molecules, 22, 7: 13 doi: http://dx.doi.org/10.3390/molecules22071174
Zhang, F., Ma, H.J., Bowatte, K., Kwiatkowski, D., Mittmann, E., Qasem, H., Krau, N., Zeng, X.L., Ren, Z., Scheerer, P., Yang, X.J. and Lamparter, T. (2017). Crystal Structures of Bacterial (6-4) Photolyase Mutants with Impaired DNA Repair Activity. Photochem Photobiol Sci, 93, 1: 304-314 doi: http://dx.doi.org/10.1111/php.12699
Zhang, M., Bommer, M., Chatterjee, R., Hussein, R., Yano, J., Dau, H., Kern, J., Dobbek, H. and Zouni, A. (2017). Structural insights into the light-driven auto-assembly process of the water-oxidizing Mn(4)CaO(5)-cluster in photosystem II. Elife, 6, doi: http://dx.doi.org/10.7554/eLife.26933

2018 back up ↑

Adam, S. and Bondar, A.N. (2018). Mechanism by which water and protein electrostatic interactions control proton transfer at the active site of channelrhodopsin. PLoS One, 13, 8: e0201298 doi: http://dx.doi.org/10.1371/journal.pone.0201298
Adam, S., Knapp-Mohammady, M., Yi, J. and Bondar, A.N. (2018). Revised CHARMM force field parameters for iron-containing cofactors of photosystem II. J Comput Chem, 39, 1: 7-20 doi: http://dx.doi.org/10.1002/jcc.24918
Balke, J., Volz, P., Neumann, F., Brodwolf, R., Wolf, A., Pischon, H., Radbruch, M., Mundhenk, L., Gruber, A.D., Ma, N. and Alexiev, U. (2018). Visualizing Oxidative Cellular Stress Induced by Nanoparticles in the Subcytotoxic Range Using Fluorescence Lifetime Imaging. Small, 14, 23: 11 doi: http://dx.doi.org/10.1002/smll.201800310
Batebi, H., Dragelj, J. and Imhof, P. (2018). Role of AP-endonuclease (Ape1) active site residues in stabilization of the reactant enzyme-DNA complex. Proteins, 86, 4: 439-453 doi: http://dx.doi.org/10.1002/prot.25460
Baumann, T., Schmitt, F.J., Pelzer, A., Spiering, V.J., Freiherr von Sass, G.J., Friedrich, T. and Budisa, N. (2018). Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence. J Vis Exp, 134: doi: http://dx.doi.org/10.3791/57017
Borchert, A., Kalms, J., Roth, S.R., Rademacher, M., Schmidt, A., Holzhutter, H.G., Kuhn, H. and Scheerer, P. (2018). Crystal structure and functional characterization of selenocysteine-containing glutathione peroxidase 4 suggests an alternative mechanism of peroxide reduction. Biochim Biophys Acta Mol Cell Biol Lipids, 1863, 9: 1095-1107 doi: http://dx.doi.org/10.1016/j.bbalip.2018.06.006
Bräunig, J., Dinter, J., Höfig, C.S., Paisdzior, S., Szczepek, M., Scheerer, P., Rosowski, M., Mittag, J., Kleinau, G. and Biebermann, H. (2018). The Trace Amine-Associated Receptor 1 Agonist 3-lodothyronamine Induces Biased Signaling at the Serotonin 1 b Receptor. Front Pharmacol, 9, 11 doi: http://dx.doi.org/10.3389/fphar.2018.00222
Buhrke, D., Kuhlmann, U., Michael, N. and Hildebrandt, P. (2018). The Photoconversion of Phytochrome Includes an Unproductive Shunt Reaction Pathway. ChemPhysChem, 19, 5: 566-570 doi: http://dx.doi.org/10.1002/cphc.201701311
Daldrop, J.O., Kappler, J., Brünig, F.N. and Netz, R.R. (2018). Butane dihedral angle dynamics in water is dominated by internal friction. PNAS, 115, 20: 5169-5174 doi: http://dx.doi.org/10.1073/pnas.1722327115
Daldrop, J.O., Saita, M., Heyden, M., Lorenz-Fonfria, V.A., Heberle, J. and Netz, R.R. (2018). Orientation of non-spherical protonated water clusters revealed by infrared absorption dichroism. Nat Commun, 9, 7 doi: http://dx.doi.org/10.1038/s41467-017-02669-9
Elgeti, M., Kazmin, R., Rose, A.S., Szczepek, M., Hildebrand, P.W., Bartl, F.J., Scheerer, P. and Hofmann, K.P. (2018). The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin. J Biol Chem, 293, 12: 4403-4410 doi: http://dx.doi.org/10.1074/jbc.M117.817890
Elghobashi-Meinhardt, N., Phatak, P., Bondar, A.N., Elstner, M. and Smith, J.C. (2018). Catalysis of Ground State cis trans Isomerization of Bacteriorhodopsin's Retinal Chromophore by a Hydrogen-Bond Network. J Membr Biol, 251, 3: 315-327 doi: http://dx.doi.org/10.1007/s00232-018-0027-x
Geiger, M.A., Jagtap, A.P., Kaushik, M., Sun, H., Stöppler, D., Sigurdsson, S.T., Corzilius, B. and Oschkinat, H. (2018). Efficiency of Water-Soluble Nitroxide Biradicals for Dynamic Nuclear Polarization in Rotating Solids at 9.4 T: bcTol-M and cyolyl-TOTAPOL as New Polarizing Agents. Chem-Eur J, 24, 51: 13485-13494 doi: http://dx.doi.org/10.1002/chem.201801251
Ghane, T., Gorriz, R.F., Wrzalek, S., Volkenandt, S., Dalatieh, F., Reidelbach, M. and Imhof, P. (2018). Hydrogen-Bonded Network and Water Dynamics in the D-channel of Cytochrome c Oxidase. J Membr Biol, 251, 3: 299-314 doi: http://dx.doi.org/10.1007/s00232-018-0019-x
Grimm, C., Silapetere, A., Vogt, A., Sierra, Y.A.B. and Hegemann, P. (2018). Electrical properties, substrate specificity and optogenetic potential of the engineered light-driven sodium pump eKR2. Sci Rep, 8, 12 doi: http://dx.doi.org/10.1038/s41598-018-27690-w
Guerra, F., Siemers, M., Mielack, C. and Bondar, A.N. (2018). Dynamics of Long-Distance Hydrogen-Bond Networks in Photosystem II. J Phys Chem B, 122, 17: 4625-4641 doi: http://dx.doi.org/10.1021/acs.jpcb.8b00649
Guo, Y.A., Wolff, F.E., Schapiro, I., Elstner, M. and Marazzi, M. (2018). Different hydrogen bonding environments of the retinal protonated Schiff base control the photoisomerization in channelrhodopsin-2. Phys Chem Chem Phys, 20, 43: 27501-27509 doi: http://dx.doi.org/10.1039/c8cp05210g
Harris, A., Saita, M., Resler, T., Hughes-Visentin, A., Maia, R., Pranga-Sellnau, F., Bondar, A.N., Heberle, J. and Brown, L.S. (2018). Molecular details of the unique mechanism of chloride transport by a cyanobacterial rhodopsin. Phys Chem Chem Phys, 20, 5: 3184-3199 doi: http://dx.doi.org/10.1039/c7cp06068h
Hu, H.D., Ataka, K., Menny, A., Fourati, Z., Sauguet, L., Corringer, P.J., Koehl, P., Heberle, J. and Delarue, M. (2018). Electrostatics, proton sensor, and networks governing the gating transition in GLIC, a proton-gated pentameric ion channel. Proc Natl Acad Sci U S A, 115, 52: E12172-E12181 doi: http://dx.doi.org/10.1073/pnas.1813378116
Hussein, R., Ibrahim, M., Chatterjee, R., Coates, L., Müh, F., Yachandra, V.K., Yano, J., Kern, J., Dobbek, H. and Zouni, A. (2018). Optimizing Crystal Size of Photosystem II by Macroseeding: Toward Neutron Protein Crystallography. Cryst Growth Des, 18, 1: 85-94 doi: http://dx.doi.org/10.1021/acs.cgd.7b00878
Kern, J., Chatterjee, R., Young, I.D., Fuller, F.D., Lassalle, L., Ibrahim, M., Gul, S., Fransson, T., Brewster, A.S., Alonso-Mori, R., Hussein, R., Zhang, M., Douthit, L., de Lichtenberg, C., Cheah, M.H., Shevela, D., Wersig, J., Seuffert, I., Sokaras, D., Pastor, E., Weninger, C., Kroll, T., Sierra, R.G., Aller, P., Butryn, A., Orville, A.M., Liang, M.N., Batyuk, A., Koglin, J.E., Carbajo, S., Boutet, S., Moriarty, N.W., Holton, J.M., Dobbek, H., Adams, P.D., Bergmann, U., Sauter, N.K., Zouni, A., Messinger, J., Yano, J. and Yachandra, V.K. (2018). Structures of the intermediates of Kok's photosynthetic water oxidation clock. Nature, 563, 7731: 421-+ doi: http://dx.doi.org/10.1038/s41586-018-0681-2
Mamatkulov, S.I., Rinne, K.F., Buchner, R., Netz, R.R. and Bonthuis, D.J. (2018). Water-separated ion pairs cause the slow dielectric mode of magnesium sulfate solutions. J Chem Phys, 148, 22: 222812 doi: http://dx.doi.org/10.1063/1.5000385
Nogly, P., Weinert, T., James, D., Carbajo, S., Ozerov, D., Furrer, A., Gashi, D., Borin, V., Skopintsev, P., Jaeger, K., Nass, K., Bath, P., Bosman, R., Koglin, J., Seaberg, M., Lane, T., Kekilli, D., Brunle, S., Tanaka, T., Wu, W., Milne, C., White, T., Barty, A., Weierstall, U., Panneels, V., Nango, E., Iwata, S., Hunter, M., Schapiro, I., Schertler, G., Neutze, R. and Standfuss, J. (2018). Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science, 361, 6398: doi: http://dx.doi.org/10.1126/science.aat0094
Oda, K., Vierock, J., Oishi, S., Rodriguez-Rozada, S., Taniguchi, R., Yamashita, K., Wiegert, J.S., Nishizawa, T., Hegemann, P. and Nureki, O. (2018). Crystal structure of the red light-activated channelrhodopsin Chrimson. Nat Commun, 9, 11 doi: http://dx.doi.org/10.1038/s41467-018-06421-9
Pfitzner, E., Seki, H., Schlesinger, R., Ataka, K. and Heberle, J. (2018). Disc Antenna Enhanced Infrared Spectroscopy: From Self-Assembled Monolayers to Membrane Proteins. ACS Sens, 3, 5: 984-991 doi: http://dx.doi.org/10.1021/acssensors.8b00139
Reidelbach, M., Weber, M. and Imhof, P. (2018). Prediction of perturbed proton transfer networks. PLoS One, 13, 12: e0207718 doi: http://dx.doi.org/10.1371/journal.pone.0207718
Rossini, E., Bochevarov, A.D. and Knapp, E.W. (2018). Empirical Conversion of pK_a Values between Different Solvents and Interpretation of the Parameters: Application to Water, Acetonitrile, Dimethyl Sulfoxide, and Methanol. ACS Omega, 3, 2: 1653-1662 doi: http://dx.doi.org/10.1021/acsomega.7b01895
Saita, M., Pranga-Sellnau, F., Resler, T., Schlesinger, R., Heberle, J. and Lorenz-Fonfria, V.A. (2018). Photoexcitation of the P₄⁴⁸⁰ State Induces a Secondary Photocycle That Potentially Desensitizes Channelrhodopsin-2. J Am Chem Soc, 140, 31: 9899-9903 doi: http://dx.doi.org/10.1021/jacs.8b03931
Saleh, N., Kleinau, G., Heyder, N., Clark, T., Hildebrand, P.W. and Scheerer, P. (2018). Binding, Thermodynamics, and Selectivity of a Non-peptide Antagonist to the Melanocortin-4 Receptor. Front Pharmacol, 9, 10 doi: http://dx.doi.org/10.3389/fphar.2018.00560
Scheerer, P., Unger, E. and Tian, L. (2018). Protein structures guide the design of a much-needed tool for neuroscience. Nature, 561, 7723: 312-313 doi: http://dx.doi.org/10.1038/d41586-018-06670-0
Scheib, U., Broser, M., Constantin, O.M., Yang, S., Gao, S.Q., Mukherjee, S., Stehfest, K., Nagel, G., Gee, C.E. and Hegemann, P. (2018). Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain. Nat Commun, 9, 15 doi: http://dx.doi.org/10.1038/s41467-018-04428-w
Schmidt, A., Sauthof, L., Szczepek, M., Lopez, M.F., Escobar, F.V., Qureshi, B.M., Michael, N., Buhrke, D., Stevens, T., Kwiatkowski, D., Von Stetten, D., Mroginski, M.A., Krauss, N., Lamparter, T., Hildebrandt, P. and Scheerer, P. (2018). Structural snapshot of a bacterial phytochrome in its functional intermediate state. Nat Commun, 9, 13 doi: http://dx.doi.org/10.1038/s41467-018-07392-7
Schnedermann, C., Yang, X., Liebel, M., Spillane, K.M., Lugtenburg, J., Fernandez, I., Valentini, A., Schapiro, I., Olivucci, M., Kukura, P. and Mathies, R.A. (2018). Evidence for a vibrational phase-dependent isotope effect on the photochemistry of vision. Nat Chem, 10, 4: 449-455 doi: http://dx.doi.org/10.1038/s41557-018-0014-y
Schultz, B.J., Mohrmann, H., Lorenz-Fonfria, V.A. and Heberle, J. (2018). Protein dynamics observed by tunable mid-IR quantum cascade lasers across the time range from 10 ns to 1 s. Spectroc Acta Pt A-Molec Biomolec Spectr, 188, 666-674 doi: http://dx.doi.org/10.1016/j.saa.2017.01.010
Schuth, N., Zaharieva, I., Chernev, P., Berggren, G., Anderlund, M., Styring, S., Dau, H. and Haumann, M. (2018). Kα X-ray Emission Spectroscopy on the Photosynthetic Oxygen-Evolving Complex Supports Manganese Oxidation and Water Binding in the S₃ State. Inorg Chem, 57, 16: 10424-10430 doi: http://dx.doi.org/10.1021/acs.inorgchem.8b01674
Song, C., Mroginski, M.A., Lang, C., Kopycki, J., Gartner, W., Matysik, J. and Hughes, J. (2018). 3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function. Front Plant Sci, 9, 498 doi: http://dx.doi.org/10.3389/fpls.2018.00498
Stöppler, D., Macpherson, A., Smith-Penzel, S., Basse, N., Lecomte, F., Deboves, H.A., Taylor, R.D., Norman, T., Porter, J., Waters, L.C., Westwood, M., Cossins, B., Cain, K., White, J., Griffin, R., Prosser, C., Kelm, S., Sullivan, A.H., Fox, D., Carr, M.D., Henry, A., Taylor, R., Meier, B.H., Oschkinat, H. and Lawson, A.D. (2018). Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR. PLoS Biol, 16, 5: 27 doi: http://dx.doi.org/10.1371/journal.pbio.2006192
Sullivan, B., Archibald, R., Langan, P.S., Dobbek, H., Bommer, M., McFeeters, R.L., Coates, L., Wang, X.P., Gallmeier, F., Carpenter, J.M., Lynch, V. and Langan, P. (2018). Improving the accuracy and resolution of neutron crystallographic data by three-dimensional profile fitting of Bragg peaks in reciprocal space. Acta Crystallogr Sect D-Struct Biol, 74, 1085-1095 doi: http://dx.doi.org/10.1107/s2059798318013347
Utesch, T., Catalina, A.D., Schattenberg, C., Paege, N., Schmieder, P., Krause, E., Miao, Y.L., McCammon, A., Meyer, V., Jung, S. and Mroginski, M.A. (2018). A Computational Modeling Approach Predicts Interaction of the Antifungal Protein AFP from Aspergillus giganteus with Fungal Membranes via Its γ-Core Motif. mSphere, 3, 5: 15 doi: http://dx.doi.org/10.1128/mSphere.00377-18

2019 back up ↑

Abrashev, M.V., Chernev, P., Kubella, P., Mohammadi, M.R., Pasquini, C., Dau, H. and Zaharieva, I. (2019). Origin of the heat-induced improvement of catalytic activity and stability of MnO_x electrocatalysts for water oxidation. J Mater Chem A, 7, 28: 17022-17036 doi: http://dx.doi.org/10.1039/c9ta05108b
Assunçao, R., Zaharieva, I. and Dau, H. (2019). Ammonia as a substrate-water analogue in photosynthetic water oxidation: Influence on activation barrier of the O₂-formation step. Biochim Biophys Acta Bioenerg, 1860, 7: 533-540 doi: http://dx.doi.org/10.1016/j.bbabio.2019.04.005
Baumann, T., Hauf, M., Schildhauer, F., Eberl, K.B., Durkin, P.M., Deniz, E., Löffler, J.G., Acevedo-Rocha, C.G., Jaric, J., Martins, B.M., Dobbek, H., Bredenbeck, J. and Budisa, N. (2019). Site-Resolved Observation of Vibrational Energy Transfer Using a Genetically Encoded Ultrafast Heater. Angew Chem-Int Edit, 58, 9: 2899-2903 doi: http://dx.doi.org/10.1002/anie.201812995
Bondar, A.N. and Lemieux, M.J. (2019). Reactions at Biomembrane Interfaces. Chem Rev, 119, 9: 6162-6183 doi: http://dx.doi.org/10.1021/acs.chemrev.8b00596
Buhrke, D., Tavraz, N.N., Shcherbakova, D.M., Sauthof, L., Moldenhauer, M., Velazquez Escobar, F., Verkhusha, V.V., Hildebrandt, P. and Friedrich, T. (2019). Chromophore binding to two cysteines increases quantum yield of near-infrared fluorescent proteins. Sci Rep, 9, 1: 1866 doi: http://dx.doi.org/10.1038/s41598-018-38433-2
Chatterjee, R., Lassalle, L., Gul, S., Fuller, F.D., Young, I.D., Ibrahim, M., de Lichtenberg, C., Cheah, M.H., Zouni, A., Messinger, J., Yachandra, V.K., Kern, J. and Yano, J. (2019). Structural isomers of the S₂ state in photosystem II: do they exist at room temperature and are they important for function? Physiol Plant, 166, 1: 60-72 doi: http://dx.doi.org/10.1111/ppl.12947
Ehrenberg, D., Krause, N., Saita, M., Bamann, C., Kar, R.K., Hoffmann, K., Heinrich, D., Schapiro, I., Heberle, J. and Schlesinger, R. (2019). Atomistic Insight into the Role of Threonine 127 in the Functional Mechanism of Channelrhodopsin-2. Appl Sci-Basel, 9, 22: 4905 doi: http://dx.doi.org/10.3390/app9224905
Ehrenberg, D., Varma, N., Deupi, X., Koyanagi, M., Terakita, A., Schertler, G.F.X., Heberle, J. and Lesca, E. (2019). The Two-Photon Reversible Reaction of the Bistable Jumping Spider Rhodopsin-1. Biophys J, 116, 7: 1248-1258 doi: http://dx.doi.org/10.1016/j.bpj.2019.02.025
Fernandez Lopez, M., Nguyen, A.D., Velazquez Escobar, F., Gonzalez, R., Michael, N., Nogacz, Z., Piwowarski, P., Bartl, F., Siebert, F., Heise, I., Scheerer, P., Gartner, W., Mroginski, M.A. and Hildebrandt, P. (2019). Role of the Propionic Side Chains for the Photoconversion of Bacterial Phytochromes. Biochemistry, 58, 33: 3504-3519 doi: http://dx.doi.org/10.1021/acs.biochem.9b00526
Fudim, R., Szczepek, M., Vierock, J., Vogt, A., Schmidt, A., Kleinau, G., Fischer, P., Bartl, F., Scheerer, P. and Hegemann, P. (2019). Design of a light-gated proton channel based on the crystal structure of Coccomyxa rhodopsin. Sci Signal, 12, 573: 11 doi: http://dx.doi.org/10.1126/scisignal.aav4203
Giliberti, V., Polito, R., Ritter, E., Broser, M., Hegemann, P., Puskar, L., Schade, U., Zanetti-Polzi, L., Daidone, I., Corni, S., Rusconi, F., Biagioni, P., Baldassarre, L. and Ortolani, M. (2019). Tip-Enhanced Infrared Difference-Nanospectroscopy of the Proton Pump Activity of Bacteriorhodopsin in Single Purple Membrane Patches. Nano Lett, 19, 5: 3104-3114 doi: http://dx.doi.org/10.1021/acs.nanolett.9b00512
González, R. and Mroginski, M.A. (2019). Fully Quantum Chemical Treatment of Chromophore-Protein Interactions in Phytochromes. J Phys Chem B, 123, 46: 9819-9830 doi: http://dx.doi.org/10.1021/acs.jpcb.9b08938
Götz, R., Ly, K.H., Wrzolek, P., Dianat, A., Croy, A., Cuniberti, G., Hildebrandt, P., Schwalbe, M. and Weidinger, I.M. (2019). Influence of Mesityl and Thiophene Peripheral Substituents on Surface Attachment, Redox Chemistry, and ORR Activity of Molecular Iron Porphyrin Catalysts on Electrodes. Inorg Chem, 58, 16: 10637-10647 doi: http://dx.doi.org/10.1021/acs.inorgchem.9b00043
Gravelle, S., Netz, R.R. and Bocquet, L. (2019). Adsorption Kinetics in Open Nanopores as a Source of Low-Frequency Noise. Nano Lett, 19, 10: 7265-7272 doi: http://dx.doi.org/10.1021/acs.nanolett.9b02858
Han, R.C., Rempfer, K., Zhang, M., Dobbek, H., Zouni, A., Dau, H. and Luber, S. (2019). Investigating the Structure and Dynamics of Apo-Photosystem II. ChemCatChem, 11, 16: 4072-4080 doi: http://dx.doi.org/10.1002/cctc.201900351
Karathanou, K. and Bondar, A.N. (2019). Using Graphs of Dynamic Hydrogen-Bond Networks To Dissect Conformational Coupling in a Protein Motor. J Chem Inf Model, 59, 5: 1882-1896 doi: http://dx.doi.org/10.1021/acs.jcim.8b00979
Karathanou, K., Lazaratos, M., Siemers, M. and Bondar, A.N. (2019). Role of Dynamic Hydrogen-Bond Networks in Protein Allostery. Biophys J, 116, 3: 498A-498A doi: http://dx.doi.org/10.1016/j.bpj.2018.11.2687
Kemmler, L., Ibrahim, M., Dobbek, H., Zouni, A. and Bondar, A.N. (2019). Dynamic water bridging and proton transfer at a surface carboxylate cluster of photosystem II. Phys Chem Chem Phys, 21, 45: 25449-25466 doi: http://dx.doi.org/10.1039/c9cp03926k
Krause, B.S., Kaufmann, J.C.D., Kuhne, J., Vierock, J., Huber, T., Sakmar, T.P., Gerwert, K., Bartl, F.J. and Hegemann, P. (2019). Tracking Pore Hydration in Channelrhodopsin by Site-Directed Infrared-Active Azido Probes. Biochemistry, 58, 9: 1275-1286 doi: http://dx.doi.org/10.1021/acs.biochem.8b01211
Kuhne, J., Vierock, J., Tennigkeit, S.A., Dreier, M.A., Wietek, J., Petersen, D., Gavriljuk, K., El-Mashtoly, S.F., Hegemann, P. and Gerwert, K. (2019). Unifying photocycle model for light adaptation and temporal evolution of cation conductance in channelrhodopsin-2. Proc Natl Acad Sci U S A, 116, 19: 9380-9389 doi: http://dx.doi.org/10.1073/pnas.1818707116
Loche, P., Ayaz, C., Schlaich, A., Uematsu, Y. and Netz, R.R. (2019). Giant Axial Dielectric Response in Water-Filled Nanotubes and Effective Electrostatic Ion-Ion Interactions from a Tensorial Dielectric Model. J Phys Chem B, 123, 50: 10850-10857 doi: http://dx.doi.org/10.1021/acs.jpcb.9b09269
Loche, P., Wolde-Kidan, A., Schlaich, A., Bonthuis, D.J. and Netz, R.R. (2019). Comment on "Hydrophobic Surface Enhances Electrostatic Interaction in Water". Physical Review Letters, 123, 4: 049601 doi: http://dx.doi.org/10.1103/PhysRevLett.123.049601
Luck, M., Escobar, F.V., Glass, K., Sabotke, M.I., Hagedorn, R., Corellou, F., Siebert, F., Hildebrandt, P. and Hegemann, P. (2019). Photoreactions of the Histidine Kinase Rhodopsin Ot-HKR from the Marine Picoalga Ostreococcus tauri. Biochemistry, 58, 14: 1878-1891 doi: http://dx.doi.org/10.1021/acs.biochem.8b01200
Mukherjee, S., Hegemann, P. and Broser, M. (2019). Enzymerhodopsins: novel photoregulated catalysts for optogenetics. Curr Opin Struct Biol, 57, 118-126 doi: http://dx.doi.org/10.1016/j.sbi.2019.02.003
Muller, M., Lauster, D., Wildenauer, H.H.K., Herrmann, A. and Block, S. (2019). Mobility-Based Quantification of Multivalent Virus-Receptor Interactions: New Insights Into Influenza A Virus Binding Mode. Nano Lett, 19, 3: 1875-1882 doi: http://dx.doi.org/10.1021/acs.nanolett.8b04969
Nass Kovacs, G., Colletier, J.P., Grünbein, M.L., Yang, Y., Stensitzki, T., Batyuk, A., Carbajo, S., Doak, R.B., Ehrenberg, D., Foucar, L., Gasper, R., Gorel, A., Hilpert, M., Kloos, M., Koglin, J.E., Reinstein, J., Roome, C.M., Schlesinger, R., Seaberg, M., Shoeman, R.L., Stricker, M., Boutet, S., Haacke, S., Heberle, J., Heyne, K., Domratcheva, T., Barends, T.R.M. and Schlichting, I. (2019). Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin. Nat Commun, 10, 1: 3177 doi: http://dx.doi.org/10.1038/s41467-019-10758-0
Oppermann, J., Fischer, P., Silapetere, A., Liepe, B., Rodriguez-Rozada, S., Flores-Uribe, J., Peter, E., Keidel, A., Vierock, J., Kaufmann, J., Broser, M., Luck, M., Bartl, F., Hildebrandt, P., Wiegert, J.S., Béjà, O., Hegemann, P. and Wietek, J. (2019). MerMAIDs: a family of metagenomically discovered marine anion-conducting and intensely desensitizing channelrhodopsins. Nat Commun, 10, 13 doi: http://dx.doi.org/10.1038/s41467-019-11322-6
Parveen, N., Rydell, G.E., Larson, G., Hytonen, V.P., Zhdanov, V.P., Hook, F. and Block, S. (2019). Competition for Membrane Receptors: Norovirus Detachment via Lectin Attachment. J Am Chem Soc, 141, 41: 16303-16311 doi: http://dx.doi.org/10.1021/jacs.9b06036
Pasquini, C., Zaharieva, I., González-Flores, D., Chernev, P., Mohammadi, M.R., Guidoni, L., Smith, R.D.L. and Dau, H. (2019). H/D Isotope Effects Reveal Factors Controlling Catalytic Activity in Co-Based Oxides for Water Oxidation. J Am Chem Soc, 141, 7: 2938-2948 doi: http://dx.doi.org/10.1021/jacs.8b10002
Riedel, M., Wersig, J., Ruff, A., Schuhmann, W., Zouni, A. and Lisdat, F. (2019). A Z-Scheme-Inspired Photobioelectrochemical H₂O/O₂ Cell with a 1 V Open-Circuit Voltage Combining Photosystem II and PbS Quantum Dots. Angew Chem-Int Edit, 58, 3: 801-805 doi: http://dx.doi.org/10.1002/anie.201811172
Senger, M., Eichmann, V., Laun, K., Duan, J.F., Wittkamp, F., Knör, G., Apfel, U.P., Happe, T., Winkler, M., Heberle, J. and Stripp, S.T. (2019). How FeFe -Hydrogenase Facilitates Bidirectional Proton Transfer. J Am Chem Soc, 141, 43: 17394-17403 doi: http://dx.doi.org/10.1021/jacs.9b09225
Sidabras, J.W., Duan, J.F., Winkler, M., Happe, T., Hussein, R., Zouni, A., Suter, D., Schnegg, A., Lubitz, W. and Reijerse, E.J. (2019). Extending electron paramagnetic resonance to nanoliter volume protein single crystals using a self-resonant microhelix. Sci Adv, 5, 10: 11 doi: http://dx.doi.org/10.1126/sciadv.aay1394
Siemers, M., Lazaratos, M., Karathanou, K., Guerra, F., Brown, L.S. and Bondar, A.N. (2019). Bridge: A Graph-Based Algorithm to Analyze Dynamic H-Bond Networks in Membrane Proteins. J Chem Theory Comput, 15, 12: 6781-6798 doi: http://dx.doi.org/10.1021/acs.jctc.9b00697
Vogt, A., Silapetere, A., Grimm, C., Heiser, F., Möller, M.A. and Hegemann, P. (2019). Engineered Passive Potassium Conductance in the KR2 Sodium Pump. Biophys J, 116, 10: 1941-1951 doi: http://dx.doi.org/10.1016/j.bpj.2019.04.001
Wiebeler, C., Rao, A.G., Gartner, W. and Schapiro, I. (2019). The Effective Conjugation Length Is Responsible for the Red/Green Spectral Tuning in the Cyanobacteriochrome Slr1393g3. Angew Chem Int Ed Engl, 58, 7: 1934-1938 doi: http://dx.doi.org/10.1002/anie.201810266
Wolde-Kidan, A., Pham, Q.D., Schlaich, A., Loche, P., Sparr, E., Netz, R.R. and Schneck, E. (2019). Influence of polar co-solutes and salt on the hydration of lipid membranes. Phys Chem Chem Phys, 21, 31: 16989-17000 doi: http://dx.doi.org/10.1039/c9cp01953g
Zaharieva, I. and Dau, H. (2019). Energetics and Kinetics of S-State Transitions Monitored by Delayed Chlorophyll Fluorescence. Front Plant Sci, 10, 386 doi: http://dx.doi.org/10.3389/fpls.2019.00386

2020 back up ↑

Balos, V., Imoto, S., Netz, R.R., Bonn, M., Bonthuis, D.J., Nagata, Y. and Hunger, J. (2020). Macroscopic conductivity of aqueous electrolyte solutions scales with ultrafast microscopic ion motions. Nat Commun, 11, 1: 8 doi: http://dx.doi.org/10.1038/s41467-020-15450-2
Battocchio, G., González, R., Rao, A.G., Schapiro, I. and Mroginski, M.A. (2020). Dynamic Properties of the Photosensory Domain of Deinococcus radiodurans Bacteriophytochrome. J Phys Chem B, 124, 9: 1740-1750 doi: http://dx.doi.org/10.1021/acs.jpcb.0c00612
Bertalan, É., Lesnik, S., Bren, U. and Bondar, A.N. (2020). Protein-water hydrogen-bond networks of G protein-coupled receptors: Graph-based analyses of static structures and molecular dynamics. J Struct Biol, 212, 3: 16 doi: http://dx.doi.org/10.1016/j.jsb.2020.107634
Broser, M., Spreen, A., Konold, P.E., Peter, E., Adam, S., Borin, V., Schapiro, I., Seifert, R., Kennis, J.T.M., Sierra, Y.A.B. and Hegemann, P. (2020). NeoR, a near-infrared absorbing rhodopsin. Nat Commun, 11, 1: 10 doi: http://dx.doi.org/10.1038/s41467-020-19375-8
Buhrke, D., Battocchio, G., Wilkening, S., Blain-Hartung, M., Baumann, T., Schmitt, F.J., Friedrich, T., Mroginski, M.A. and Hildebrandt, P. (2020). Red, Orange, Green: Light- and Temperature-Dependent Color Tuning in a Cyanobacteriochrome. Biochemistry, 59, 4: 509-519 doi: http://dx.doi.org/10.1021/acs.biochem.9b00931
Buhrke, D., Gourinchas, G., Müller, M., Michael, N., Hildebrandt, P. and Winkler, A. (2020). Distinct chromophore-protein environments enable asymmetric activation of a bacteriophytochrome-activated diguanylate cyclase. J Biol Chem, 295, 2: 539-551 doi: http://dx.doi.org/10.1074/jbc.RA119.011915
Buhrke, D. and Hildebrandt, P. (2020). Probing Structure and Reaction Dynamics of Proteins Using Time-Resolved Resonance Raman Spectroscopy. Chem Rev, 120, 7: 3577-3630 doi: http://dx.doi.org/10.1021/acs.chemrev.9b00429
Chernev, P., Fischer, S., Hoffmann, J., Oliver, N., Assuncao, R., Yu, B., Burnap, R.L., Zaharieva, I., Nürnberg, D.J., Haumann, M. and Dau, H. (2020). Light-driven formation of manganese oxide by today's photosystem II supports evolutionarily ancient manganese-oxidizing photosynthesis. Nat Commun, 11, 1: 6110 doi: http://dx.doi.org/10.1038/s41467-020-19852-0
Escobar, F.V., Kneip, C., Michael, N., Hildebrandt, T., Tavraz, N., Gärtner, W., Hughes, J., Friedrich, T., Scheerer, P., Mroginski, M.A. and Hildebrandt, P. (2020). The Lumi-R Intermediates of Prototypical Phytochromes. J Phys Chem B, 124, 20: 4044-4055 doi: http://dx.doi.org/10.1021/acs.jpcb.0c01059
Friedrich, D., Brünig, F.N., Nieuwkoop, A.J., Netz, R.R., Hegemann, P. and Oschkinat, H. (2020). Collective exchange processes reveal an active site proton cage in bacteriorhodopsin. Commun Biol, 3, 1: 9 doi: http://dx.doi.org/10.1038/s42003-019-0733-7
Friedrich, D., Perodeau, J., Nieuwkoop, A.J. and Oschkinat, H. (2020). MAS NMR detection of hydrogen bonds for protein secondary structure characterization. J Biomol NMR, 74, 4-5: 247-256 doi: http://dx.doi.org/10.1007/s10858-020-00307-z
Gerland, L., Friedrich, D., Hopf, L., Donovan, E.J., Wallmann, A., Erdmann, N., Diehl, A., Bommer, M., Buzar, K., Ibrahim, M., Schmieder, P., Dobbek, H., Zouni, A., Bondar, A.N., Dau, H. and Oschkinat, H. (2020). pH-Dependent Protonation of Surface Carboxylate Groups in PsbO Enables Local Buffering and Triggers Structural Changes. Chembiochem, 21, 11: 1597-1604 doi: http://dx.doi.org/10.1002/cbic.201900739
Golub, M., Hussein, R., Ibrahim, M., Hecht, M., Wieland, D.C.F., Martel, A., Machado, B., Zouni, A. and Pieper, J. (2020). Solution Structure of the Detergent-Photosystem II Core Complex Investigated by Small-Angle Scattering Techniques. J Phys Chem B, 124, 39: 8583-8592 doi: http://dx.doi.org/10.1021/acs.jpcb.0c07169
Harris, A., Lazaratos, M., Siemers, M., Watt, E., Hoang, A., Tomida, S., Schubert, L., Saita, M., Heberle, J., Furutani, Y., Kandori, H., Bondar, A.N. and Brown, L.S. (2020). Mechanism of Inward Proton Transport in an Antarctic Microbial Rhodopsin. J Phys Chem B, 124, 24: 4851-4872 doi: http://dx.doi.org/10.1021/acs.jpcb.0c02767
Hontani, Y., Broser, M., Luck, M., Weissenborn, J., Kloz, M., Hegemann, P. and Kennis, J.T.M. (2020). Dual Photoisomerization on Distinct Potential Energy Surfaces in a UV-Absorbing Rhodopsin. J Am Chem Soc, 142, 26: 11464-11473 doi: http://dx.doi.org/10.1021/jacs.0c03229
Hugentobler, K.G., Heinrich, D., Berg, J., Heberle, J., Brzezinski, P., Schlesinger, R. and Block, S. (2020). Lipid Composition Affects the Efficiency in the Functional Reconstitution of the Cytochrome c Oxidase. Int J Mol Sci, 21, 19: doi: http://dx.doi.org/10.3390/ijms21196981
Ibrahim, M., Fransson, T., Chatterjee, R., Cheah, M.H., Hussein, R., Lassalle, L., Sutherlin, K.D., Young, I.D., Fuller, F.D., Gul, S., Kim, I.S., Simon, P.S., de Lichtenberg, C., Chernev, P., Bogacz, I., Pham, C.C., Orville, A.M., Saichek, N., Northen, T., Batyuk, A., Carbajo, S., Alonso-Mori, R., Tono, K., Owada, S., Bhowmick, A., Bolotovsky, R., Mendez, D., Moriarty, N.W., Holton, J.M., Dobbek, H., Brewster, A.S., Adams, P.D., Sauter, N.K., Bergmann, U., Zouni, A., Messinger, J., Kern, J., Yachandra, V.K. and Yano, J. (2020). Untangling the sequence of events during the S₂ → S₃ transition in photosystem II and implications for the water oxidation mechanism. Proc Natl Acad Sci U S A, 117, 23: 12624-12635 doi: http://dx.doi.org/10.1073/pnas.2000529117
Karathanou, K., Kemmler, L., Lazaratos, M., Siemers, M. and Bondar, A.N. (2020). Proton Binding at Protein and Membrane Interfaces. Biophys J, 118, 3: 179A-179A doi:
Kaufmann, J.C.D., Krause, B.S., Adam, S., Ritter, E., Schapiro, I., Hegemann, P. and Bartl, F.J. (2020). Modulation of Light Energy Transfer from Chromophore to Protein in the Channelrhodopsin ReaChR. Biophys J, 119, 3: 705-716 doi: http://dx.doi.org/10.1016/j.bpj.2020.06.031
Kraskov, A., Nguyen, A.D., Goerling, J., Buhrke, D., Velazquez Escobar, F., Fernandez Lopez, M., Michael, N., Sauthof, L., Schmidt, A., Piwowarski, P., Yang, Y., Stensitzki, T., Adam, S., Bartl, F., Schapiro, I., Heyne, K., Siebert, F., Scheerer, P., Mroginski, M.A. and Hildebrandt, P. (2020). Intramolecular Proton Transfer Controls Protein Structural Changes in Phytochrome. Biochemistry, 59, 9: 1023-1037 doi: http://dx.doi.org/10.1021/acs.biochem.0c00053
Kruse, F., Nguyen, A.D., Dragelj, J., Schlesinger, R., Heberle, J., Mroginski, M.A. and Weidinger, I.M. (2020). Author Correction: Characterisation of the Cyanate Inhibited State of Cytochrome c Oxidase. Sci Rep, 10, 1: 6853 doi: http://dx.doi.org/10.1038/s41598-020-63869-w
Kruse, F., Nguyen, A.D., Dragelj, J., Schlesinger, R., Heberle, J., Mroginski, M.A. and Weidinger, I.M. (2020). Characterisation of the Cyanate Inhibited State of Cytochrome c Oxidase. Sci Rep, 10, 1: 10 doi: http://dx.doi.org/10.1038/s41598-020-60801-0
Lazaratos, M., Karathanou, K. and Bondar, A.N. (2020). Graphs of dynamic H-bond networks: from model proteins to protein complexes in cell signaling. Curr Opin Struct Biol, 64, 79-87 doi: http://dx.doi.org/10.1016/j.sbi.2020.06.006
Mäusle, S.M., Abzaliyeva, A., Greife, P., Simon, P.S., Perez, R., Zilliges, Y. and Dau, H. (2020). Activation energies for two steps in the S₂ → S₃ transition of photosynthetic water oxidation from time-resolved single-frequency infrared spectroscopy. J Chem Phys, 153, 21: 14 doi: http://dx.doi.org/10.1063/5.0027995
Müh, F. and Zouni, A. (2020). Structural basis of light-harvesting in the photosystem II core complex. Protein Sci, 29, 5: 1090-1119 doi: http://dx.doi.org/10.1002/pro.3841
Nagano, S., Guan, K.L., Shenkutie, S.M., Feiler, C., Weiss, M., Kraskov, A., Buhrke, D., Hildebrandt, P. and Hughes, J. (2020). Structural insights into photoactivation and signalling in plant phytochromes. Nat Plants, 6, 5: 16 doi: http://dx.doi.org/10.1038/s41477-020-0638-y
Reidelbach, M. and Imhof, P. (2020). Proton transfer in the D-channel of cytochrome c oxidase modeled by a transition network approach. Biochim Biophys Acta-Gen Subj, 1864, 8: 10 doi: http://dx.doi.org/10.1016/j.bbagen.2020.129614
Rozenberg, A., Oppermann, J., Wietek, J., Fernandez Lahore, R.G., Sandaa, R.A., Bratbak, G., Hegemann, P. and Beja, O. (2020). Lateral Gene Transfer of Anion-Conducting Channelrhodopsins between Green Algae and Giant Viruses. Curr Biol, 30, 24: 4910-4920 e4915 doi: http://dx.doi.org/10.1016/j.cub.2020.09.056
Sadeghi, M., Balke, J., Schneider, C., Nagano, S., Stellmacher, J., Lochnit, G., Lang, C., Weise, C., Hughes, J. and Alexiev, U. (2020). Transient Deprotonation of the Chromophore Affects Protein Dynamics Proximal and Distal to the Linear Tetrapyrrole Chromophore in Phytochrome Cph1. Biochemistry, 59, 9: 1051-1062 doi: http://dx.doi.org/10.1021/acs.biochem.9b00967
Skopintsev, P., Ehrenberg, D., Weinert, T., James, D., Kar, R.K., Johnson, P.J.M., Ozerov, D., Furrer, A., Martiel, I., Dworkowski, F., Nass, K., Knopp, G., Cirelli, C., Arrell, C., Gashi, D., Mous, S., Wranik, M., Gruhl, T., Kekilli, D., Brünle, S., Deupi, X., Schertler, G.F.X., Benoit, R.M., Panneels, V., Nogly, P., Schapiro, I., Milne, C., Heberle, J. and Standfuss, J. (2020). Femtosecond-to-millisecond structural changes in a light-driven sodium pump. Nature, 583, 7815: 314-+ doi: http://dx.doi.org/10.1038/s41586-020-2307-8
Slavov, C., Fischer, T., Barnoy, A., Shin, H., Rao, A.G., Wiebeler, C., Zeng, X.L., Sun, Y.F., Xu, Q.Z., Gutt, A., Zhao, K.H., Gärtner, W., Yang, X.J., Schapiro, I. and Wachtveitl, J. (2020). The interplay between chromophore and protein determines the extended excited state dynamics in a single-domain phytochrome. Proc Natl Acad Sci U S A, 117, 28: 16356-16362 doi: http://dx.doi.org/10.1073/pnas.192170611
Stauffer, M., Hirschi, S., Ucurum, Z., Harder, D., Schlesinger, R. and Fotiadis, D. (2020). Engineering and Production of the Light-Driven Proton Pump Bacteriorhodopsin in 2D Crystals for Basic Research and Applied Technologies. Methods Protoc, 3, 3: 22 doi: http://dx.doi.org/10.3390/mps3030051
Stensitzki, T., Adam, S., Schlesinger, R., Schapiro, I. and Heyne, K. (2020). Ultrafast Backbone Protonation in Channelrhodopsin-1 Captured by Polarization Resolved Fs Vis-pump-IR-Probe Spectroscopy and Computational Methods. Molecules, 25, 4: 848 doi: http://dx.doi.org/10.3390/molecules25040848
Wolf, A., Dragelj, J., Wonneberg, J., Stellmacher, J., Balke, J., Woelke, A.L., Hodoscek, M., Knapp, E.W. and Alexiev, U. (2020). The redox-coupled proton-channel opening in cytochrome c oxidase. Chem Sci, 11, 15: 3804-3811 doi: http://dx.doi.org/10.1039/c9sc06463j
Wolf, A., Wonneberg, J., Balke, J. and Alexiev, U. (2020). Electronation-dependent structural change at the proton exit side of cytochrome c oxidase as revealed by site-directed fluorescence labeling. FEBS J, 287, 6: 1232-1246 doi: http://dx.doi.org/10.1111/febs.15084
Xu, X.L., Por, A., Wiebeler, C., Zhao, K.H., Schapiro, I. and Gärtner, W. (2020). Structural elements regulating the photochromicity in a cyanobacteriochrome. Proc Natl Acad Sci U S A, 117, 5: 2432-2440 doi: http://dx.doi.org/10.1073/pnas.1910208117

2021 back up ↑

Adam, S., Wiebeler, C. and Schapiro, I. (2021). Structural Factors Determining the Absorption Spectrum of Channelrhodopsins: A Case Study of the Chimera C1C2. J Chem Theory Comput, 17, 10: 6302-6313 doi: http://dx.doi.org/10.1021/acs.jctc.1c00160
Asido, M., Kar, R.K., Kriebel, C.N., Braun, M., Glaubitz, C., Schapiro, I. and Wachtveitl, J. (2021). Transient Near-UV Absorption of the Light-Driven Sodium Pump Krokinobacter eikastus Rhodopsin 2: A Spectroscopic Marker for Retinal Configuration. J Phys Chem Lett, 12, 27: 6284-6291 doi: http://dx.doi.org/10.1021/acs.jpclett.1c01436
Baserga, F., Dragelj, J., Kozuch, J., Mohrmann, H., Knapp, E.W., Stripp, S.T. and Heberle, J. (2021). Quantification of Local Electric Field Changes at the Active Site of Cytochrome c Oxidase by Fourier Transform Infrared Spectroelectrochemical Titrations. Front Chem, 9, 13 doi: http://dx.doi.org/10.3389/fchem.2021.669452
Bertalan, É., Lesca, E., Schertler, G.F.X. and Bondar, A.N. (2021). C-Graphs Tool with Graphical User Interface to Dissect Conserved Hydrogen-Bond Networks: Applications to Visual Rhodopsins. J Chem Inf Model, 61, 11: 5692-5707 doi: http://dx.doi.org/10.1021/acs.jcim.1c00827
Bondar, A.N. (2021). Proton-Binding Motifs of Membrane-Bound Proteins: From Bacteriorhodopsin to Spike Protein S. Front Chem, 9, 8 doi: http://dx.doi.org/10.3389/fchem.2021.685761
Chen, Y.Y., Krämer, A., Charron, N.E., Husic, B.E., Clementi, C. and Noé, F. (2021). Machine learning implicit solvation for molecular dynamics. J Chem Phys, 155, 8: 14 doi: http://dx.doi.org/10.1063/5.0059915
Dong, P., Stellmacher, J., Bouchet, L.M., Nieke, M., Kumar, A., Osorio-Blanco, E.R., Nagel, G., Lohan, S.B., Teutloff, C., Patzelt, A., Schafer-Korting, M., Calderon, M., Meinke, M.C. and Alexiev, U. (2021). A Dual Fluorescence-Spin Label Probe for Visualization and Quantification of Target Molecules in Tissue by Multiplexed FLIM-EPR Spectroscopy. Angew Chem Int Ed Engl, 60, 27: 14938-14944 doi: http://dx.doi.org/10.1002/anie.202012852
Dragelj, J., Mroginski, M.A. and Knapp, E.W. (2021). Beating Heart of Cytochrome c Oxidase: The Shared Proton of Heme a₃ Propionates. J Phys Chem B, 125, 34: 9668-9677 doi: http://dx.doi.org/10.1021/acs.jpcb.1c03619
Fischer, P., Mukherjee, S., Peter, E., Broser, M., Bartl, F. and Hegemann, P. (2021). The inner mechanics of rhodopsin guanylyl cyclase during cGMP-formation revealed by real-time FTIR spectroscopy. Elife, 10, 31 doi: http://dx.doi.org/10.7554/eLife.71384; 10.7554/eLife.71384.sa1; 10.7554/eLife.71384.sa2
Fransson, T., Alonso-Mori, R., Chatterjee, R., Cheah, M.H., Ibrahim, M., Hussein, R., Zhang, M., Fuller, F., Gul, S., Kim, I.S., Simon, P.S., Bogacz, I., Makita, H., de Lichtenberg, C., Song, S.H., Batyuk, A., Sokaras, D., Massad, R., Doyle, M., Britz, A., Weninger, C., Zouni, A., Messinger, J., Yachandra, V.K., Yano, J., Kern, J. and Bergmann, U. (2021). Effects of x-ray free-electron laser pulse intensity on the Mn Kβ_1,3 x-ray emission spectrum in photosystem II-A case study for metalloprotein crystals and solutions. Struct Dyn-US, 8, 6: 13 doi: http://dx.doi.org/10.1063/4.0000130
Golub, M., Kölsch, A., Feoktystov, A., Zouni, A. and Pieper, J. (2021). Insights into Solution Structures of Photosynthetic Protein Complexes from Small-Angle Scattering Methods. Crystals, 11, 2: 16 doi: http://dx.doi.org/10.3390/cryst11020203
Gonella, G., Backus, E.H.G., Nagata, Y., Bonthuis, D.J., Loche, P., Schlaich, A., Netz, R.R., Kühnle, A., McCrum, I.T., Koper, M.T.M., Wolf, M., Winter, B., Meijer, G., Campen, R.K. and Bonn, M. (2021). Water at charged interfaces. Nat Rev Chem, 5, 7: 466-485 doi: http://dx.doi.org/10.1038/s41570-021-00293-2
Hontani, Y., Baloban, M., Escobar, F.V., Jansen, S.A., Shcherbakova, D.M., Weissenborn, J., Kloz, M., Mroginski, M.A., Verkhusha, V.V. and Kennis, J.T.M. (2021). Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome. Comm Chem, 4, 1: 11 doi: http://dx.doi.org/10.1038/s42004-020-00437-3
Hussein, R., Ibrahim, M., Bhowmick, A., Simon, P.S., Chatterjee, R., Lassalle, L., Doyle, M., Bogacz, I., Kim, I.S., Cheah, M.H., Gul, S., de Lichtenberg, C., Chernev, P., Pham, C.C., Young, I.D., Carbajo, S., Fuller, F.D., Alonso-Mori, R., Batyuk, A., Sutherlin, K.D., Brewster, A.S., Bolotovsky, R., Mendez, D., Holton, J.M., Moriarty, N.W., Adams, P.D., Bergmann, U., Sauter, N.K., Dobbek, H., Messinger, J., Zouni, A., Kern, J., Yachandra, V.K. and Yano, J. (2021). Structural dynamics in the water and proton channels of photosystem II during the S₂ to S₃ transition. Nat Commun, 12, 1: 16 doi: http://dx.doi.org/10.1038/s41467-021-26781-z
Ibrahim, M., Moriarty, N.W., Kern, J., Holton, J.M., Brewster, A.S., Bhowmick, A., Bergmann, U., Zouni, A., Messinger, J., Yachandra, V.K., Yano, J., Dobbek, H., Sauter, N.K. and Adams, P.D. (2021). Reply to Wang et al.: Clear evidence of binding of Ox to the oxygen-evolving complex of photosystem II is best observed in the omit map. Proc Natl Acad Sci U S A, 118, 24: doi: http://dx.doi.org/10.1073/pnas.2102342118
Juarez, J.F.B., Judge, P.J., Adam, S., Axford, D., Vinals, J., Birch, J., Kwan, T.O.C., Hoi, K.K., Yen, H.Y., Vial, A., Milhiet, P.E., Robinson, C.V., Schapiro, I., Moraes, I. and Watts, A. (2021). Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization. Nat Commun, 12, 1: 10 doi: http://dx.doi.org/10.1038/s41467-020-20596-0
Keable, S.M., Kolsch, A., Simon, P.S., Dasgupta, M., Chatterjee, R., Subramanian, S.K., Hussein, R., Ibrahim, M., Kim, I.S., Bogacz, I., Makita, H., Pham, C.C., Fuller, F.D., Gul, S., Paley, D., Lassalle, L., Sutherlin, K.D., Bhowmick, A., Moriarty, N.W., Young, I.D., Blaschke, J.P., de Lichtenberg, C., Chernev, P., Cheah, M.H., Park, S., Park, G., Kim, J., Lee, S.J., Park, J., Tono, K., Owada, S., Hunter, M.S., Batyuk, A., Oggenfuss, R., Sander, M., Zerdane, S., Ozerov, D., Nass, K., Lemke, H., Mankowsky, R., Brewster, A.S., Messinger, J., Sauter, N.K., Yachandra, V.K., Yano, J., Zouni, A. and Kern, J. (2021). Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I. Sci Rep, 11, 1: 21787 doi: http://dx.doi.org/10.1038/s41598-021-00236-3
Kozuch, J., Schneider, S.H., Zheng, C., Ji, Z., Bradshaw, R.T. and Boxer, S.G. (2021). Testing the Limitations of MD-Based Local Electric Fields Using the Vibrational Stark Effect in Solution: Penicillin G as a Test Case. J Phys Chem B, 125, 17: 4415-4427 doi: http://dx.doi.org/10.1021/acs.jpcb.1c00578
Kraskov, A., Buhrke, D., Scheerer, P., Shaef, I., Sanchez, J.C., Carrillo, M., Noda, M., Feliz, D., Stojkovic, E.A. and Hildebrandt, P. (2021). On the Role of the Conserved Histidine at the Chromophore Isomerization Site in Phytochromes. J Phys Chem B, 125, 50: 13696-13709 doi: http://dx.doi.org/10.1021/acs.jpcb.1c08245
Kraskov, A., von Sass, J., Nguyen, A.D., Hoang, T.O., Buhrke, D., Katz, S., Michael, N., Kozuch, J., Zebger, I., Siebert, F., Scheerer, P., Mroginski, M.A., Budisa, N. and Hildebrandt, P. (2021). Local Electric Field Changes during the Photoconversion of the Bathy Phytochrome Agp2. Biochemistry, 60, 40: 2967-2977 doi: http://dx.doi.org/10.1021/acs.biochem.1c00426
Kruse, F., Nguyen, A.D., Dragelj, J., Heberle, J., Hildebrandt, P., Mroginski, M.A. and Weidinger, I.M. (2021). A Resonance Raman Marker Band Characterizes the Slow and Fast Form of Cytochrome c Oxidase. J Am Chem Soc, 143, 7: 2769-2776 doi: http://dx.doi.org/10.1021/jacs.0c10767
Lamparter, T., Xue, P., Elkurdi, A., Kaeser, G., Sauthof, L., Scheerer, P. and Krauss, N. (2021). Phytochromes in Agrobacterium fabrum. Front Plant Sci, 12, 642801 doi: http://dx.doi.org/10.3389/fpls.2021.642801
Lesnik, S., Bertalan, E., Bren, U. and Bondar, A.N. (2021). Opioid Receptors and Protonation-Coupled Binding of Opioid Drugs. Int J Mol Sci, 22, 24: 18 doi: http://dx.doi.org/10.3390/ijms222413353
Maia, R.N.A., Ehrenberg, D., Oldemeyer, S., Knieps-Grunhagen, E., Krauss, U. and Heberle, J. (2021). Real-Time Tracking of Proton Transfer from the Reactive Cysteine to the Flavin Chromophore of a Photosensing Light Oxygen Voltage Protein. J Am Chem Soc, 143, 32: 12535-12542 doi: http://dx.doi.org/10.1021/jacs.1c03409
Merga, G., Lopez, M.F., Fischer, P., Piwowarski, P., Nogacz, Z., Kraskov, A., Buhrke, D., Escobar, F.V., Michael, N., Siebert, F., Scheerer, P., Bartl, F. and Hildebrandt, P. (2021). Light- and temperature-dependent dynamics of chromophore and protein structural changes in bathy phytochrome Agp2. Phys Chem Chem Phys, 23, 33: 18197-18205 doi: http://dx.doi.org/10.1039/d1cp02494a
Morlock, S., Subramanian, S.K., Zouni, A. and Lisdat, F. (2021). Scalable Three-Dimensional Photobioelectrodes Made of Reduced Graphene Oxide Combined with Photosystem I. ACS Appl Mater Interfaces, 13, 9: 11237-11246 doi: http://dx.doi.org/10.1021/acsami.1c01142
Mroginski, M.A., Adam, S., Amoyal, G.S., Barnoy, A., Bondar, A.N., Borin, V.A., Church, J.R., Domratcheva, T., Ensing, B., Fanelli, F., Ferré, N., Filiba, O., Pedraza-González, L., González, R., González-Espinoza, C.E., Kar, R.K., Kemmler, L., Kim, S.S., Kongsted, J., Krylov, A.I., Lahav, Y., Lazaratos, M., NasserEddin, Q., Navizet, I., Nemukhin, A., Olivucci, M., Olsen, J.M.H., Ortíz, A.P.D., Pieri, E., Rao, A.G., Rhee, Y.M., Ricardi, N., Sen, S., Solov'yov, I.A., De Vico, L., Wesolowski, T.A., Wiebeler, C., Yang, X.C. and Schapiro, I. (2021). Frontiers in Multiscale Modeling of Photoreceptor Proteins. Photochem Photobiol Sci, 97, 2: 243-269 doi: http://dx.doi.org/10.1111/php.13372
Oda, K., Nomura, T., Nakane, T., Yamashita, K., Inoue, K., Ito, S., Vierock, J., Hirata, K., Maturana, A.D., Katayama, K., Ikuta, T., Ishigami, I., Izume, T., Umeda, R., Eguma, R., Oishi, S., Kasuya, G., Kato, T., Kusakizako, T., Shihoya, W., Shimada, H., Takatsuji, T., Takemoto, M., Taniguchi, R., Tomita, A., Nakamura, R., Fukuda, M., Miyauchi, H., Lee, Y., Nango, E., Tanaka, R., Tanaka, T., Sugahara, M., Kimura, T., Shimamura, T., Fujiwara, T., Yamanaka, Y., Owada, S., Joti, Y., Tono, K., Ishitani, R., Hayashi, S., Kandori, H., Hegemann, P., Iwata, S., Kubo, M., Nishizawa, T. and Nureki, O. (2021). Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin. Elife, 10, doi: http://dx.doi.org/10.7554/eLife.62389
Otero, L.H., Foscaldi, S., Antelo, G.T., Rosano, G.L., Sirigu, S., Klinke, S., Defelipe, L.A., Sánchez-Lamas, M., Battocchio, G., Conforte, V., Vojnov, A.A., Chavas, L.M.G., Goldbaum, F.A., Mroginski, M.A., Rinaldi, J. and Bonomi, H.R. (2021). Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level. Sci Adv, 7, 48: 22 doi: http://dx.doi.org/10.1126/sciadv.abh1097
Riebe, S., Adam, S., Roy, B., Maisuls, I., Daniliuc, C.G., Dubbert, J., Strassert, C.A., Schapiro, I. and Voskuhl, J. (2021). Bridged Aromatic Oxo- and Thioethers with Intense Emission in Solution and the Solid State. Chem-Asian J, 16, 16: 2307-2313 doi: http://dx.doi.org/10.1002/asia.202100492
Siemers, M. and Bondar, A.N. (2021). Interactive Interface for Graph-Based Analyses of Dynamic H-Bond Networks: Application to Spike Protein S. J Chem Inf Model, 61, 6: 2998-3014 doi: http://dx.doi.org/10.1021/acs.jcim.1c00306
Sokolovski, S.G., Zherebtsov, E.A., Kar, R.K., Golonka, D., Stabel, R., Chichkov, N.B., Gorodetsky, A., Schapiro, I., Möglich, A. and Rafailov, E.U. (2021). Two-photon conversion of a bacterial phytochrome. Biophys J, 120, 5: 964-974 doi: http://dx.doi.org/10.1016/j.bpj.2021.01.028
Theiß, M., Grupe, M., Lamparter, T., Mroginski, M.A. and Diller, R. (2021). Ultrafast proton release reaction and primary photochemistry of phycocyanobilin in solution observed with fs-time-resolved mid-IR and UV/Vis spectroscopy. Photochem Photobiol Sci, 20, 6: 715-732 doi: http://dx.doi.org/10.1007/s43630-021-00045-7
Walter, M. and Schlesinger, R. (2021). Nanodisc Reconstitution of Channelrhodopsins Heterologously Expressed in Pichia pastoris for Biophysical Investigations. Methods Mol Biol, 2191, 29-48 doi: http://dx.doi.org/10.1007/978-1-0716-0830-2_3
Wang, J., Charron, N., Husic, B., Olsson, S., Noé, F. and Clementi, C. (2021). Multi-body effects in a coarse-grained protein force field. J Chem Phys, 154, 16: 11 doi: http://dx.doi.org/10.1063/5.0041022
Xue, P., Bai, Y.N., Rottwinkel, G., Averbukh, E., Ma, Y.Y., Roeder, T., Scheerer, P., Krauss, N. and Lamparter, T. (2021). Phytochrome Mediated Responses in Agrobacterium fabrum: Growth, Motility and Plant Infection. Curr Microbiol, 78, 7: 2708-2719 doi: http://dx.doi.org/10.1007/s00284-021-02526-5

2022 back up ↑

Allgower, F., Gamiz-Hernandez, A.P., Rutherford, A.W. and Kaila, V.R.I. (2022). Molecular Principles of Redox-Coupled Protonation Dynamics in Photosystem II. J Am Chem Soc, 144, 16: 7171-7180 doi: http://dx.doi.org/10.1021/jacs.1c13041
Ataka, K., Baumann, A., Chen, J.L., Redlich, A., Heberle, J. and Schlesinger, R. (2022). Monitoring the Progression of Cell-Free Expression of Microbial Rhodopsins by Surface Enhanced IR Spectroscopy: Resolving a Branch Point for Successful/Unsuccessful Folding. Front Mol Biosci, 9, 929285 doi: http://dx.doi.org/10.3389/fmolb.2022.929285
Baidukova, O., Oppermann, J., Kelterborn, S., Fernandez Lahore, R.G., Schumacher, D., Evers, H., Kamrani, Y.Y. and Hegemann, P. (2022). Gating and ion selectivity of Channelrhodopsins are critical for photo-activated orientation of Chlamydomonas as shown by in vivo point mutation. Nat Commun, 13, 1: 7253 doi: http://dx.doi.org/10.1038/s41467-022-35018-6
Baserga, F., Vorkas, A., Crea, F., Schubert, L., Chen, J.L., Redlich, A., La Greca, M., Storm, J., Oldemeyer, S., Hoffmann, K., Schlesinger, R. and Heberle, J. (2022). Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy. Front Mol Biosci, 9, 915328 doi: http://dx.doi.org/10.3389/fmolb.2022.915328
Bondar, A.N. (2022). Graphs of Hydrogen-Bond Networks to Dissect Protein Conformational Dynamics. J Phys Chem B, 126, 22: 3973-3984 doi: http://dx.doi.org/10.1021/acs.jpcb.2c00200
Bondar, A.N. (2022). Interplay between local protein interactions and water bridging of a proton antenna carboxylate cluster. Biochim Biophys Acta Biomembr, 1864, 12: 184052 doi: http://dx.doi.org/10.1016/j.bbamem.2022.184052
Brünig, F.N., Daldrop, J.O. and Netz, R.R. (2022). Pair-Reaction Dynamics in Water: Competition of Memory, Potential Shape, and Inertial Effects. J Phys Chem B, 126, 49: 10295-10304 doi: http://dx.doi.org/10.1021/acs.jpcb.2c05923
Brünig, F.N., Geburtig, O., von Canal, A., Kappler, J. and Netz, R.R. (2022). Time-Dependent Friction Effects on Vibrational Infrared Frequencies and Line Shapes of Liquid Water. J Phys Chem B, 126, 7: 1579-1589 doi: http://dx.doi.org/10.1021/acs.jpcb.1c09481
Brünig, F.N., Hillmann, P., Kim, W.K., Daldrop, J.O. and Netz, R.R. (2022). Proton-transfer spectroscopy beyond the normal-mode scenario. J Chem Phys, 157, 17: 174116 doi: http://dx.doi.org/10.1063/5.0116686
Brünig, F.N., Netz, R.R. and Kappler, J. (2022). Barrier-crossing times for different non-Markovian friction in well and barrier: A numerical study. Phys Rev E, 106, 4: 20 doi: http://dx.doi.org/10.1103/PhysRevE.106.044133
Brünig, F.N., Rammler, M., Adams, E.M., Havenith, M. and Netz, R.R. (2022). Spectral signatures of excess-proton waiting and transfer-path dynamics in aqueous hydrochloric acid solutions. Nat Commun, 13, 1: 12 doi: http://dx.doi.org/10.1038/s41467-022-31700-x
Crea, F., Vorkas, A., Redlich, A., Cruz, R., Shi, C., Trauner, D., Lange, A., Schlesinger, R. and Heberle, J. (2022). Photoactivation of a Mechanosensitive Channel. Front Mol Biosci, 9, 905306 doi: http://dx.doi.org/10.3389/fmolb.2022.905306
Emiliani, V., Entcheva, E., Hedrich, R., Hegemann, P., Konrad, K.R., Luscher, C., Mahn, M., Pan, Z.H., Sims, R.R., Vierock, J. and Yizhar, O. (2022). Optogenetics for light control of biological systems. Nat Rev Methods Primers, 2, 1: doi: http://dx.doi.org/10.1038/s43586-022-00136-4
Fernandez Lahore, R.G., Pampaloni, N.P., Schiewer, E., Heim, M.M., Tillert, L., Vierock, J., Oppermann, J., Walther, J., Schmitz, D., Owald, D., Plested, A.J.R., Rost, B.R. and Hegemann, P. (2022). Calcium-permeable channelrhodopsins for the photocontrol of calcium signalling. Nat Commun, 13, 1: 7844 doi: http://dx.doi.org/10.1038/s41467-022-35373-4
Golub, M., Gatcke, J., Subramanian, S., Kolsch, A., Darwish, T., Howard, J.K., Feoktystov, A., Matsarskaia, O., Martel, A., Porcar, L., Zouni, A. and Pieper, J. (2022). "Invisible" Detergents Enable a Reliable Determination of Solution Structures of Native Photosystems by Small-Angle Neutron Scattering. J Phys Chem B, 126, 15: 2824-2833 doi: http://dx.doi.org/10.1021/acs.jpcb.2c01591
Heyne, K. (2022). Impact of Ultrafast Electric Field Changes on Photoreceptor Protein Dynamics. J Phys Chem B, 126, 3: 581-587 doi: http://dx.doi.org/10.1021/acs.jpcb.1c08131
Karathanou, K., Lazaratos, M., Bertalan, E., Siemers, M. and Bondar, A.N. (2022). Conformational coupling and proton binding with dynamic hydrogen-bond networks. Biophys J, 121, 3: 170a-170a doi: http://dx.doi.org/10.1016/j.bpj.2021.11.1886
La Greca, M., Chen, J.L., Schubert, L., Kozuch, J., Berneiser, T., Terpitz, U., Heberle, J. and Schlesinger, R. (2022). The Photoreaction of the Proton-Pumping Rhodopsin 1 From the Maize Pathogenic Basidiomycete Ustilago maydis. Front Mol Biosci, 9, 826990 doi: http://dx.doi.org/10.3389/fmolb.2022.826990
Lazaratos, M., Siemers, M., Brown, L.S. and Bondar, A.N. (2022). Conserved hydrogen-bond motifs of membrane transporters and receptors. Biochim Biophys Acta Biomembr, 1864, 6: 183896 doi: http://dx.doi.org/10.1016/j.bbamem.2022.183896
Liese, S., Schlaich, A. and Netz, R.R. (2022). Dielectric constant of aqueous solutions of proteins and organic polymers from molecular dynamics simulations. J Chem Phys, 156, 22: 224902 doi: http://dx.doi.org/10.1063/5.0089397
Lopez, M.F., Dahl, M., Escobar, F.V., Bonomi, H.R., Kraskov, A., Michael, N., Mroginski, M.A., Scheerer, P. and Hildebrandt, P. (2022). Photoinduced reaction mechanisms in prototypical and bathy phytochromes. Phys Chem Chem Phys, 24, 19: 11967-11978 doi: http://dx.doi.org/10.1039/d2cp00020b
Mous, S., Gotthard, G., Ehrenberg, D., Sen, S., Weinert, T., Johnson, P.J.M., James, D., Nass, K., Furrer, A., Kekilli, D., Ma, P., Brunle, S., Casadei, C.M., Martiel, I., Dworkowski, F., Gashi, D., Skopintsev, P., Wranik, M., Knopp, G., Panepucci, E., Panneels, V., Cirelli, C., Ozerov, D., Schertler, G.F.X., Wang, M., Milne, C., Standfuss, J., Schapiro, I., Heberle, J. and Nogly, P. (2022). Dynamics and mechanism of a light-driven chloride pump. Science, 375, 6583: 845-851 doi: http://dx.doi.org/10.1126/science.abj6663
Nagano, S., Sadeghi, M., Balke, J., Fleck, M., Heckmann, N., Psakis, G. and Alexiev, U. (2022). Improved fluorescent phytochromes for in situ imaging. Sci Rep, 12, 1: 5587 doi: http://dx.doi.org/10.1038/s41598-022-09169-x
Oliver, N., Avramov, A.P., Nürnberg, D.J., Dau, H. and Burnap, R.L. (2022). From manganese oxidation to water oxidation: assembly and evolution of the water-splitting complex in photosystem II. Photosynth Res, 152, 2: 107-133 doi: http://dx.doi.org/10.1007/s11120-022-00912-z
Palombo, R., Barneschi, L., Pedraza-Gonzalez, L., Padula, D., Schapiro, I. and Olivucci, M. (2022). Retinal chromophore charge delocalization and confinement explain the extreme photophysics of Neorhodopsin. Nat Commun, 13, 1: 6652 doi: http://dx.doi.org/10.1038/s41467-022-33953-y
Rao, A.G. and Schapiro, I. (2022). Photoisomerization of phytochrome chromophore models: an XMS-CASPT2 study. Phys Chem Chem Phys, 24, 48: 29393-29405 doi: http://dx.doi.org/10.1039/d2cp04249e
Rodriguez-Rozada, S., Wietek, J., Tenedini, F., Sauter, K., Dhiman, N., Hegemann, P., Soba, P. and Wiegert, J.S. (2022). Aion is a bistable anion-conducting channelrhodopsin that provides temporally extended and reversible neuronal silencing. Commun Biol, 5, 1: 687 doi: http://dx.doi.org/10.1038/s42003-022-03636-x
Sadeghi, M., Balke, J., Rafaluk-Mohr, T. and Alexiev, U. (2022). Long-Distance Protonation-Conformation Coupling in Phytochrome Species. Molecules, 27, 23: 15 doi: http://dx.doi.org/10.3390/molecules27238395
Saura, P., Riepl, D., Frey, D.M., Wikstrom, M. and Kaila, V.R.I. (2022). Electric fields control water-gated proton transfer in cytochrome c oxidase. Proc Natl Acad Sci U S A, 119, 38: e2207761119 doi: http://dx.doi.org/10.1073/pnas.2207761119
Schubert, L., Langner, P., Ehrenberg, D., Lorenz-Fonfria, V.A. and Heberle, J. (2022). Protein conformational changes and protonation dynamics probed by a single shot using quantum-cascade-laser-based IR spectroscopy. J Chem Phys, 156, 20: 204201 doi: http://dx.doi.org/10.1063/5.0088526
Silapetere, A., Hwang, S., Hontani, Y., Fernandez Lahore, R.G., Balke, J., Escobar, F.V., Tros, M., Konold, P.E., Matis, R., Croce, R., Walla, P.J., Hildebrandt, P., Alexiev, U., Kennis, J.T.M., Sun, H., Utesch, T. and Hegemann, P. (2022). QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins. Nat Commun, 13, 1: 5501 doi: http://dx.doi.org/10.1038/s41467-022-33084-4
Weaver, J.B., Kozuch, J., Kirsh, J.M. and Boxer, S.G. (2022). Nitrile Infrared Intensities Characterize Electric Fields and Hydrogen Bonding in Protic, Aprotic, and Protein Environments. J Am Chem Soc, 144, 17: 7562-7567 doi: http://dx.doi.org/10.1021/jacs.2c00675
Yaguchi, M., Jia, X., Schlesinger, R., Jiang, X., Ataka, K. and Heberle, J. (2022). Near-Infrared Activation of Sensory Rhodopsin II Mediated by NIR-to-Blue Upconversion Nanoparticles. Front Mol Biosci, 8, 782688 doi: http://dx.doi.org/10.3389/fmolb.2021.782688
Yang, Y., Stensitzki, T., Sauthof, L., Schmidt, A., Piwowarski, P., Escobar, F.V., Michael, N., Nguyen, A.D., Szczepek, M., Brünig, F.N., Netz, R.R., Mroginski, M.A., Adam, S., Bartl, F., Schapiro, I., Hildebrandt, P., Scheerer, P. and Heyne, K. (2022). Ultrafast proton-coupled isomerization in the phototransformation of phytochrome. Nat Chem, 14, 7: 823-830 doi: http://dx.doi.org/10.1038/s41557-022-00944-x
Zahn, C., Stensitzki, T. and Heyne, K. (2022). Femtosecond anisotropy excitation spectroscopy to disentangle the Q_x and Q_y absorption in chlorophyll a. Chem Sci, 13, 42: 12426-12432 doi: http://dx.doi.org/10.1039/d2sc03538c
Zheng, C., Mao, Y.Z., Kozuch, J., Atsango, A.O., Ji, Z., Markland, T.E. and Boxer, S.G. (2022). A two-directional vibrational probe reveals different electric field orientations in solution and an enzyme active site. Nat Chem, 14, 8: 891-897 doi: http://dx.doi.org/10.1038/s41557-022-00937-w

2023 back up ↑

Balke, J., Gutiérrez, P.D., Rafaluk-Mohr, T., Proksch, J., Koksch, B. and Alexiev, U. (2023). Osmolytes Modulate Photoactivation of Phytochrome: Probing Protein Hydration. Molecules, 28, 16: 11 doi: http://dx.doi.org/10.3390/molecules28166121
Baserga, F., Storm, J., Schlesinger, R., Heberle, J. and Stripp, S.T. (2023). The catalytic reaction of cytochrome c oxidase probed by in situ gas titrations and FTIR difference spectroscopy. Biochim Biophys Acta Bioenerg, 1864, 4: 149000 doi: http://dx.doi.org/10.1016/j.bbabio.2023.149000
Bhowmick, A., Hussein, R., Bogacz, I., Simon, P.S., Ibrahim, M., Chatterjee, R., Doyle, M.D., Cheah, M.H., Fransson, T., Chernev, P., Kim, I.S., Makita, H., Dasgupta, M., Kaminsky, C.J., Zhang, M., Gätcke, J., Haupt, S., Nangca, II, Keable, S.M., Aydin, A.O., Tono, K., Owada, S., Gee, L.B., Fuller, F.D., Batyuk, A., Alonso-Mori, R., Holton, J.M., Paley, D.W., Moriarty, N.W., Mamedov, F., Adams, P.D., Brewster, A.S., Dobbek, H., Sauter, N.K., Bergmann, U., Zouni, A., Messinger, J., Kern, J., Yano, J. and Yachandra, V.K. (2023). Structural evidence for intermediates during O₂ formation in photosystem II. Nature, 617, 7961: 21 doi: http://dx.doi.org/10.1038/s41586-023-06038-z
Bhowmick, A., Simon, P.S., Bogacz, I., Hussein, R., Zhang, M., Makita, H., Ibrahim, M., Chatterjee, R., Doyle, M.D., Cheah, M.H., Chernev, P., Fuller, F.D., Fransson, T., Alonso-Mori, R., Brewster, A.S., Sauter, N.K., Bergmann, U., Dobbek, H., Zouni, A., Messinger, J., Kern, J., Yachandra, V.K. and Yano, J. (2023). Going around the Kok cycle of the water oxidation reaction with femtosecond X-ray crystallography. IUCrJ, 10, Pt 6: 642-655 doi: http://dx.doi.org/10.1107/S2052252523008928
Broser, M., Andruniow, T., Kraskov, A., Palombo, R., Katz, S., Kloz, M., Dostál, J., Bernardo, C., Kennis, J.T.M., Hegemann, P., Olivucci, M. and Hildebrandt, P. (2023). Experimental Assessment of the Electronic and Geometrical Structure of a Near-Infrared Absorbing and Highly Fluorescent Microbial Rhodopsin. J Phys Chem Lett, 14, 41: 9291-9295 doi: http://dx.doi.org/10.1021/acs.jpclett.3c02167
Bühl, E., Resler, T., Lam, R., Asido, M., Bamberg, E., Schlesinger, R., Bamann, C., Heberle, J. and Wachtveitl, J. (2023). Assessing the Role of R120 in the Gating of CrChR2 by Time-Resolved Spectroscopy from Femtoseconds to Seconds. J Am Chem Soc, 145, 40: 21832-21840 doi: http://dx.doi.org/10.1021/jacs.3c05399
Dau, H. and Greife, P. (2023). Applicability of Transition State Theory to the (Proton-Coupled) Electron Transfer in Photosynthetic Water Oxidation with Emphasis on the Entropy of Activation. Inorganics, 11, 10: doi: http://dx.doi.org/10.3390/inorganics11100389
Durumeric, A.E.P., Charron, N.E., Templeton, C., Musil, F., Bonneau, K., Pasos-Trejo, A.S., Chen, Y.Y., Kelkar, A., Noé, F. and Clementi, C. (2023). Machine learned coarse-grained protein force-fields: Are we there yet? Curr Opin Struct Biol, 79, 9 doi: http://dx.doi.org/10.1016/j.sbi.2023.102533
Elkurdi, A., Guigas, G., Hourani-Alsharafat, L., Scheerer, P., Nienhaus, G.U., Krauss, N. and Lamparter, T. (2023). Time-resolved fluorescence anisotropy with Atto 488-labeled phytochrome Agp1 from Agrobacterium fabrum. Photochem Photobiol, 12 doi: http://dx.doi.org/10.1111/php.13851
Gemeinhardt, F.G., Lahav, Y., Schapiro, I., Noy, D., Müh, F., Lindorfer, D. and Renger, T. (2023). Short-Range Effects in the Special Pair of Photosystem II Reaction Centers: The Nonconservative Nature of Circular Dichroism. J Phys Chem Lett, 14, 51: 11758-11767 doi: http://dx.doi.org/10.1021/acs.jpclett.3c02693
González-Viegas, M., Kar, R.K., Miller, A.F. and Mroginski, M.A. (2023). Noncovalent interactions that tune the reactivities of the flavins in bifurcating electron transferring flavoprotein. J Biol Chem, 299, 6: 104762 doi: http://dx.doi.org/10.1016/j.jbc.2023.104762
Greife, P., Schönborn, M., Capone, M., Assunçao, R., Narzi, D., Guidoni, L. and Dau, H. (2023). The electron-proton bottleneck of photosynthetic oxygen evolution. Nature, 617, 7961: 24 doi: http://dx.doi.org/10.1038/s41586-023-06008-5
Hildebrandt, P. (2023). Vibrational Spectroscopy of Phytochromes. Biomolecules, 13, 6: 1007 doi: http://dx.doi.org/10.3390/biom13061007
Hussein, R., Ibrahim, M., Bhowmick, A., Simon, P.S., Bogacz, I., Doyle, M.D., Dobbek, H., Zouni, A., Messinger, J., Yachandra, V.K., Kern, J.F. and Yano, J. (2023). Evolutionary diversity of proton and water channels on the oxidizing side of photosystem II and their relevance to function. Photosynth Res, 158, 2: 91-107 doi: http://dx.doi.org/10.1007/s11120-023-01018-w
Kaeser, G., Krauss, N., Roughan, C., Sauthof, L., Scheerer, P. and Lamparter, T. (2023). Phytochrome-Interacting Proteins. Biomolecules, 14, 1: doi: http://dx.doi.org/10.3390/biom14010009
Kapur, B., Baldessari, F., Lazaratos, M., Nar, H., Schnapp, G., Giorgetti, A. and Bondar, A.N. (2023). Protons taken hostage: Dynamic H-bond networks of the pH-sensing GPR68. Comp Struct Biotechnol J, 21, 4370-4384 doi: http://dx.doi.org/10.1016/j.csbj.2023.08.034
Kozuch, J., Ataka, K. and Heberle, J. (2023). Surface-enhanced infrared absorption spectroscopy. Nat Rev Method Prim, 3, 1: 19 doi: http://dx.doi.org/https://doi.org/10.1038/s43586-023-00253-8
Majewski, M., Perez, A., Tholke, P., Doerr, S., Charron, N.E., Giorgino, T., Husic, B.E., Clementi, C., Noe, F. and De Fabritiis, G. (2023). Machine learning coarse-grained potentials of protein thermodynamics. Nat Commun, 14, 1: 5739 doi: http://dx.doi.org/10.1038/s41467-023-41343-1
Morlock, S., Subramanian, S.K., Zouni, A. and Lisdat, F. (2023). Closing the green gap of photosystem I with synthetic fluorophores for enhanced photocurrent generation in photobiocathodes. Chem Sci, 14, 7: 1696-1708 doi: http://dx.doi.org/10.1039/d2sc05324a
Paschke, R.R., Mohr, S., Lange, S., Lange, A. and Kozuch, J. (2023). In Situ Spectroscopic Detection of Large-Scale Reorientations of Transmembrane Helices During Influenza A M2 Channel Opening. Angew Chem Int Ed Engl, 62, 47: e202309069 doi: http://dx.doi.org/10.1002/anie.202309069
Ricardi, N., González-Espinoza, C., Adam, S., Church, J.R., Schapiro, I. and Wesolowski, T.A. (2023). Embedding Nonrigid Solutes in an Averaged Environment: A Case Study on Rhodopsins. J Chem Theory Comput, 19, 15: 5289-5302 doi: http://dx.doi.org/10.1021/acs.jctc.3c00285
Saliminasab, M., Yamazaki, Y., Palmateer, A., Harris, A., Schubert, L., Langner, P., Heberle, J., Bondar, A.N. and Brown, L.S. (2023). A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins. J Phys Chem B, 127, 37: 7872-7886 doi: http://dx.doi.org/10.1021/acs.jpcb.3c04032
Schubert, L., Chen, J.L., Fritz, T., Marxer, F., Langner, P., Hoffmann, K., Gamiz-Hernandez, A.P., Kaila, V.R.I., Schlesinger, R. and Heberle, J. (2023). Proton Release Reactions in the Inward H⁺ Pump NsXeR. J Phys Chem B, 127, 39: 8358-8369 doi: http://dx.doi.org/10.1021/acs.jpcb.3c04100
Simon, P.S., Makita, H., Bogacz, I., Fuller, F., Bhowmick, A., Hussein, R., Ibrahim, M., Zhang, M., Chatterjee, R., Cheah, M.H., Chernev, P., Doyle, M.D., Brewster, A.S., Alonso-Mori, R., Sauter, N.K., Bergmann, U., Dobbek, H., Zouni, A., Messinger, J., Kern, J., Yachandra, V.K. and Yano, J. (2023). Capturing the sequence of events during the water oxidation reaction in photosynthesis using XFELs. FEBS Lett, 597, 1: 30-37 doi: http://dx.doi.org/10.1002/1873-3468.14527
von Freiherr Sass, G.J., Blain-Hartung, M., Baumann, T., Forest, K.T., Hildebrandt, P. and Budisa, N. (2023). Orthogonal translation with 5-cyanotryptophan as an infrared probe for local structural information, electrostatics, and hydrogen bonding. Protein Sci, 32, 7: e4705 doi: http://dx.doi.org/10.1002/pro.4705
Walter, M., Schubert, L., Heberle, J., Schlesinger, R. and Losi, A. (2023). Time-resolved photoacoustics of channelrhodopsins: early energetics and light-driven volume changes. Photochem Photobiol Sci, 22, 3: 477-486 doi: http://dx.doi.org/10.1007/s43630-022-00327-8
Wolf, A., Volz-Rakebrand, P., Balke, J. and Alexiev, U. (2023). Diffusion Analysis of NAnoscopic Ensembles: A Tracking-Free Diffusivity Analysis for NAnoscopic Ensembles in Biological Samples and Nanotechnology. Small, 19, 16: e2206722 doi: http://dx.doi.org/10.1002/smll.202206722
Yang, W.F., Templeton, C., Rosenberger, D., Bittracher, A., Nüske, F., Noé, F. and Clementi, C. (2023). Slicing and Dicing: Optimal Coarse-Grained Representation to Preserve Molecular Kinetics. ACS Cent Sci, 11 doi: http://dx.doi.org/10.1021/acscentsci.2c01200
Yang, Y., Stensitzki, T., Lang, C., Hughes, J., Mroginski, M.A. and Heyne, K. (2023). Ultrafast protein response in the Pfr state of Cph1 phytochrome. Photochem Photobiol Sci, 22, 4: 919-930 doi: http://dx.doi.org/10.1007/s43630-023-00362-z
Zaporozhets, I. and Clementi, C. (2023). Multibody Terms in Protein Coarse-Grained Models: A Top-Down Perspective. J Phys Chem B, 127, 31: 6920-6927 doi: http://dx.doi.org/10.1021/acs.jpcb.3c04493

2024 back up ↑

Allgöwer, F., Pöverlein, M.C., Rutherford, A.W. and Kaila, V.R.I. (2024). Mechanism of proton release during water oxidation in Photosystem II. PNAS, 121, e2413396121: doi: http://dx.doi.org/10.1101/2024.07.03.602004
Bell, D., Lindemann, F., Gerland, L., Aucharova, H., Klein, A., Friedrich, D., Hiller, M., Grohe, K., Meier, T., van Rossum, B., Diehl, A., Hughes, J., Mueller, L.J., Linser, R., Miller, A.F. and Oschkinat, H. (2024). Sedimentation of large, soluble proteins up to 140 kDa for (1)H-detected MAS NMR and (13)C DNP NMR - practical aspects. J Biomol NMR, 78, 3: 179-192 doi: http://dx.doi.org/10.1007/s10858-024-00444-9
Blain-Hartung, M., Johannes von Sass, G., Plaickner, J., Katz, S., Tu Hoang, O., Mroginski, M.A., Esser, N., Budisa, N., Forest, K.T. and Hildebrandt, P. (2024). On the Role of a Conserved Tryptophan in the Chromophore Pocket of Cyanobacteriochrome. J Mol Biol, 436, 5: 168227 doi: http://dx.doi.org/10.1016/j.jmb.2023.168227
Dalton, B.A. and Netz, R.R. (2024). pH Modulates Friction Memory Effects in Protein Folding. Physical Review Letters, 133, 18: doi: http://dx.doi.org/10.1103/PhysRevLett.133.188401
Dekmak, M.Y., Mäusle, S.M., Brandhorst, J., Simon, P.S. and Dau, H. (2024). Tracking the first electron transfer step at the donor side of oxygen-evolving photosystem II by time-resolved infrared spectroscopy. Photosynth Res, doi: http://dx.doi.org/10.1007/s11120-023-01057-3
Fellows, A.P., Duque, A.D., Balos, V., Lehmann, L., Netz, R.R., Wolf, M. and Thamer, M. (2024). How Thick is the Air-Water Interface? - A Direct Experimental Measurement of the Decay Length of the Interfacial Structural Anisotropy. Langmuir, 40, 35: 18760-18772 doi: http://dx.doi.org/10.1021/acs.langmuir.4c02571
Fischer, P., Schiewer, E., Broser, M., Busse, W., Spreen, A., Grosse, M., Hegemann, P. and Bartl, F. (2024). The Functionality of the DC Pair in a Rhodopsin Guanylyl Cyclase from Catenaria anguillulae. J Mol Biol, 436, 5: 168375 doi: http://dx.doi.org/10.1016/j.jmb.2023.168375
Göbel, M., Ramuglia, A.R., Zhartovska, E., Budhija, V., Ly, K.H., Mroginski, M.A., Schwalbe, M. and Weidinger, I.M. (2024). Protonation of Pendant Pyridine Substituents in an Iron Porphyrin Hangman Complex: Influence on Spectral Visibility and Electrocatalysis. J Phys Chem C, 128, 18: 7624-7634 doi: http://dx.doi.org/10.1021/acs.jpcc.4c01357
Gonzalez, B.D., Forbrig, E., Yao, G., Kielb, P., Mroginski, M.A., Hildebrandt, P. and Kozuch, J. (2024). Cation Dependence of Enniatin B/Membrane-Interactions Assessed Using Surface-Enhanced Infrared Absorption (SEIRA) Spectroscopy. Chempluschem, 89, 8: e202400159 doi: http://dx.doi.org/10.1002/cplu.202400159
Hughes, J. and Winkler, A. (2024). New Insight Into Phytochromes: Connecting Structure to Function. Annu Rev Plant Biol, 75, 1: 153-183 doi: http://dx.doi.org/10.1146/annurev-arplant-070623-110636
Hussein, R., Graca, A., Forsman, J., Aydin, A.O., Hall, M., Gaetcke, J., Chernev, P., Wendler, P., Dobbek, H., Messinger, J., Zouni, A. and Schröder, W.P. (2024). Cryo-electron microscopy reveals hydrogen positions and water networks in photosystem II. Science, 384, 6702: 1349-1355 doi: http://dx.doi.org/10.1126/science.adn6541
Katz, S., Phan, H.T., Rieder, F., Seifert, F., Pietzsch, M., Laufer, J., Schmitt, F.J. and Hildebrandt, P. (2024). High Fluorescence of Phytochromes Does Not Require Chromophore Protonation. Molecules, 29, 20: doi: http://dx.doi.org/10.3390/molecules29204948
Kirsh, J.M., Weaver, J.B., Boxer, S.G. and Kozuch, J. (2024). Critical Evaluation of Polarizable and Nonpolarizable Force Fields for Proteins Using Experimentally Derived Nitrile Electric Fields. J Am Chem Soc, 146, 10: 6983-6991 doi: http://dx.doi.org/10.1021/jacs.3c14775
Mackintosh, M.J., Hoischen, D., Martin, H.D., Schapiro, I. and Gärtner, W. (2024). Merocyanines form bacteriorhodopsins with strongly bathochromic absorption maxima. Photochem Photobiol Sci, 23, 1: 31-53 doi: http://dx.doi.org/10.1007/s43630-023-00496-0
Mäusle, S.M., Agarwala, N., Eichmann, V.G., Dau, H., Nürnberg, D.J. and Hastings, G. (2024). Nanosecond time-resolved infrared spectroscopy for the study of electron transfer in photosystem I. Photosynth Res, 159, 2-3: 229-239 doi: http://dx.doi.org/10.1007/s11120-023-01035-9
Müh, F., Bothe, A. and Zouni, A. (2024). Towards understanding the crystallization of photosystem II: influence of poly(ethylene glycol) of various molecular sizes on the micelle formation of alkyl maltosides. Photosynth Res, doi: http://dx.doi.org/10.1007/s11120-024-01079-5
Nguyen, A.D., Michael, N., Sauthof, L., von Sass, J., Hoang, O.T., Schmidt, A., La Greca, M., Schlesinger, R., Budisa, N., Scheerer, P., Mroginski, M.A., Kraskov, A. and Hildebrandt, P. (2024). Hydrogen Bonding and Noncovalent Electric Field Effects in the Photoconversion of a Phytochrome. J Phys Chem B, doi: http://dx.doi.org/10.1021/acs.jpcb.4c06419
Oldemeyer, S., La Greca, M., Langner, P., Lê Công, K.L., Schlesinger, R. and Heberle, J. (2024). Nanosecond Transient IR Spectroscopy of Halorhodopsin in Living Cells. J Am Chem Soc, 146, 28: 19118-19127 doi: http://dx.doi.org/10.1021/jacs.4c03891
Oppermann, J., Rozenberg, A., Fabrin, T., Gonzalez-Cabrera, C., Parker, R., Beja, O., Prigge, M. and Hegemann, P. (2024). Robust optogenetic inhibition with red-light-sensitive anion-conducting channelrhodopsins. Elife, 12, doi: http://dx.doi.org/10.7554/eLife.90100
Poverlein, M.C., Hulm, A., Dietschreit, J.C.B., Kussmann, J., Ochsenfeld, C. and Kaila, V.R.I. (2024). QM/MM Free Energy Calculations of Long-Range Biological Protonation Dynamics by Adaptive and Focused Sampling. J Chem Theory Comput, 20, 13: 5751-5762 doi: http://dx.doi.org/10.1021/acs.jctc.4c00199
Scalfi, L., Lehmann, L., Dos Santos, A.P., Becker, M.R. and Netz, R.R. (2024). Propensity of hydroxide and hydronium ions for the air-water and graphene-water interfaces from ab initio and force field simulations. J Chem Phys, 161, 14: doi: http://dx.doi.org/10.1063/5.0226966
Shenkutie, S.M., Nagano, S. and Hughes, J. (2024). Expression, purification and crystallization of the photosensory module of phytochrome B (phyB) from Sorghum bicolor. Acta Crystallogr F Struct Biol Commun, 80, Pt 3: 59-66 doi: http://dx.doi.org/10.1107/S2053230X24000827
Sirohiwal, A., Gamiz-Hernandez, A.P. and Kaila, V.R.I. (2024). Mechanistic Principles of Hydrogen Evolution in the Membrane-Bound Hydrogenase. J Am Chem Soc, 146, 26: 18019-18031 doi: http://dx.doi.org/10.1021/jacs.4c04476
Vogt, A., Paulat, R., Parthier, D., Just, V., Szczepek, M., Scheerer, P., Xu, Q., Moglich, A., Schmitz, D., Rost, B.R. and Wenger, N. (2024). Simultaneous spectral illumination of microplates for high-throughput optogenetics and photobiology. Biol Chem, doi: http://dx.doi.org/10.1515/hsz-2023-0205

SFB 1078 - Protonation Dynamics in Protein Function

SFB 1078 - Protonation Dynamics in Protein Function

Publications

2013, 2014, 2015, 2016, 2017, 2018, 2019, 2020, 2021, 2022, 2023, 2024

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