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  Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin

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, Accepted, 1-43. doi:10.1038/s41467-019-10758-0.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-90DE-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0004-9BA4-4
Genre: Journal Article

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 Creators:
Nass Kovács, Gabriela1, Author              
Colletier, Jacques-Philippe, Author
Grünbein, Marie Luise1, Author              
Yang, Yang, Author
Stensitzki, Till, Author
Batyuk, Alexander, Author
Carbajo, Alexander, Author
Doak, R. Bruce1, Author              
Ehrenberg, David, Author
Foucar, Lutz1, Author              
Gasper, Raphael, Author
Gorel, Alexander1, Author              
Hilpert, Mario1, Author              
Kloos, Marco1, Author              
Koglin, Jason E., Author
Reinstein, Jochen1, Author              
Roome, Christopher M.1, Author              
Schlesinger, Ramona, Author
Seaberg, Matthew, Author
Shoeman, Robert L.1, Author              
Stricker, Miriam1, Author              Boutet, Sébastien, AuthorHaacke , Stefan, AuthorHeberle, Joachim, AuthorHeyne, Karsten, AuthorDomratcheva, Tatiana1, Author              Barends, Thomas R.M.1, Author              Schlichting, Ilme1, Author               more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 2018-04-182019-05-282019-07-18
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-019-10758-0
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: Accepted Sequence Number: - Start / End Page: 1 - 43 Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723