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  Chromophore twisting in the excited state of a photoswitchable fluorescent protein captured by time-resolved serial femtosecond crystallography

Coquelle, N., Sliwa, M., Woodhouse, J., Schirò, G., Adam, V., Aquila, A., et al. (2018). Chromophore twisting in the excited state of a photoswitchable fluorescent protein captured by time-resolved serial femtosecond crystallography. Nature Chemistry, 10, 31-37. doi:10.1038/nchem.2853.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-FD9C-C Version Permalink: http://hdl.handle.net/21.11116/0000-0002-CCE8-3
Genre: Journal Article

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 Creators:
Coquelle, Nicolas, Author
Sliwa, Michel, Author
Woodhouse, Joyce, Author
Schirò, Giorgio, Author
Adam, Virgile, Author
Aquila, Andrew, Author
Barends, Thomas R. M.1, Author              
Boutet, Sébastien, Author
Byrdin, Martin, Author
Carbajo, Sergio, Author
la Mora, Eugenio De, Author
Doak, R. Bruce1, Author              
Feliks, Mikolaj, Author
Fieschi, Franck, Author
Foucar, Lutz1, Author              
Guillon, Virginia, Author
Hilpert, Mario1, Author              
Hunter, Mark S., Author
Jakobs, Stefan, Author
Koglin, Jason E., Author
Kovácsová, Gabriela1, Author              Lane, Thomas J., AuthorLévy, Bernard, AuthorLiang, Mengning, AuthorNass, Karol1, Author              Ridard, Jacqueline, AuthorRobinson, Joseph S., AuthorRoome, Christopher M.1, Author              Ruckebusch, Cyril, AuthorSeaberg, Matthew, AuthorThepaut, Michel, AuthorCammarata, Marco, AuthorDemachy, Isabelle, AuthorField, Martin, AuthorShoeman, Robert L.1, Author              Bourgeois, Dominique, AuthorColletier, Jacques-Philippe, AuthorSchlichting, Ilme1, Author              Weik, Martin, Author more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Chromophores absorb light in photosensitive proteins and thereby initiate fundamental biological processes such as photosynthesis, vision and biofluorescence. An important goal in their understanding is the provision of detailed structural descriptions of the ultrafast photochemical events that they undergo, in particular of the excited states that connect chemistry to biological function. Here we report on the structures of two excited states in the reversibly photoswitchable fluorescent protein rsEGFP2. We populated the states through femtosecond illumination of rsEGFP2 in its non-fluorescent off state and observed their build-up (within less than one picosecond) and decay (on the several picosecond timescale). Using an X-ray free-electron laser, we performed picosecond time-resolved crystallography and show that the hydroxybenzylidene imidazolinone chromophore in one of the excited states assumes a near-canonical twisted configuration halfway between the trans and cis isomers. This is in line with excited-state quantum mechanics/molecular mechanics and classical molecular dynamics simulations. Our new understanding of the structure around the twisted chromophore enabled the design of a mutant that displays a twofold increase in its off-to-on photoswitching quantum yield.

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Language(s): eng - English
 Dates: 2016-03-062017-07-272017-09-112018-01-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nchem.2853
 Degree: -

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Title: Nature Chemistry
  Abbreviation : Nat. Chem.
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 10 Sequence Number: - Start / End Page: 31 - 37 Identifier: ISSN: 1755-4330
CoNE: /journals/resource/1755-4330