The conversion of light energy into a change in protein structure plays a central role in many areas of life, for example in vision or photosynthesis. The study under the direction of Prof. Dr. Ilme Schlichting, Director of the Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research was significantly supported by scientists of the SFB 1078, namely Ramona Schlesinger, Karsten Heyne and Joachim Heberle (project B4, B7 and B3) and coworkers. Within the framework of this interdisciplinary cooperation, the atomic structure of the ultra-short intermediate states of the light-driven proton pump Bacteriorhodopsin was elucidated at various points in time after photoactivation. It was shown how the molecule retinal, which is the photosensitive center of the protein, changes its structure after absorption of a photon.

Publication: 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. Nature Communications 10, Article Number 3177. doi: 10.1038/s41467-019-10758-0