Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin

Nass Kovács, Gabriela; Colletier, Jacques-Philippe; Grünbein, Marie Luise; Yang, Yang; Stensitzki, Till; Batyuk, Alexander; Carbajo, Alexander; Doak, R. Bruce; Ehrenberg, David; Foucar, Lutz; Gasper, Raphael; Gorel, Alexander; Hilpert, Mario; Kloos, Marco; Koglin, Jason E.; Reinstein, Jochen; Roome, Christopher M.; Schlesinger, Ramona; Seaberg, Matthew; Shoeman, Robert L.; Stricker, Miriam; Boutet, Sébastien; Haacke , Stefan; Heberle, Joachim; Heyne, Karsten; Domratcheva, Tatiana; Barends, Thomas R.M.; Schlichting, Ilme

doi:10.1038/s41467-019-10758-0

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin

MPS-Authors

/persons/resource/persons183396

Nass Kovács, Gabriela
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons123592

Grünbein, Marie Luise
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117878

Doak, R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92933

Foucar, Lutz
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons192083

Gorel, Alexander
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183393

Hilpert, Mario
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons203860

Kloos, Marco
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94928

Reinstein, Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183399

Roome, Christopher M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95345

Shoeman, Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons225677

Stricker, Miriam
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92695

Domratcheva, Tatiana
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92083

Barends, Thomas R.M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95189

Schlichting, Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://www.nature.com/articles/s41467-019-10758-0.pdf
(Any fulltext)

https://doi.org/10.1038/s41467-019-10758-0
(Any fulltext)

https://static-content.springer.com/esm/art%3A10.1038%2Fs41467-019-10758-0/MediaObjects/41467_2019_10758_MOESM1_ESM.pdf
(Supplementary material)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Nass Kovács, G., Colletier, J.-P., Grünbein, M. L., Yang, Y., Stensitzki, T., Batyuk, A., et al. (2019). Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin. Nature Communications, 10: 3177, pp. 1-17. doi:10.1038/s41467-019-10758-0.

Cite as: https://hdl.handle.net/21.11116/0000-0003-90DE-0

Abstract

Bacteriorhodopsin (bR) is a light-driven proton pump. The primary photochemical event upon light absorption is isomerization of the retinal chromophore. Here we used time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy were used to identify a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multiphoton effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.