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  Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy

Woodhouse, J., Nass Kovács, G., Coquelle, N., Uriarte, L. M., Adam, V., Barends, T., et al. (2020). Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy. Nature Communications, 11(741): 741, pp. 1-11. doi:10.1038/s41467-020-14537-0.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0005-A4F9-9 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0005-A4FA-8
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 Urheber:
Woodhouse, Joyce, Autor
Nass Kovács, Gabriela1, 2, Autor           
Coquelle, Nicolas, Autor
Uriarte, Lucas M., Autor
Adam, Virgile, Autor
Barends, Thomas1, 2, 3, 4, 5, 6, Autor           
Byrdin, Martin, Autor
de la Mora, Eugenio, Autor
Doak, Bruce1, 2, Autor           
Feliks, Mikolaj, Autor
Field, Martin, Autor
Fieschi, Franck, Autor
Guillon, Virginia, Autor
Jakobs, Stefan, Autor
Joti, Yasumasa, Autor
Macheboeuf, Pauline, Autor
Motomura, Koji, Autor
Nass, Karol1, 2, Autor           
Owada, Shigeki, Autor
Roome, Christopher M.1, Autor           
Ruckebusch, Cyril, AutorSchirò, Giorgio, AutorShoeman, Robert L.1, 2, 7, Autor           Thepaut, Michel, AutorTogashi, Tadashi, AutorTono, Kensuke, AutorYabashi, Makina, AutorCammarata, Marco, AutorFoucar, Lutz1, Autor           Bourgeois, Dominique, AutorSliwa, Michel, AutorColletier, Jacques-Philippe, AutorSchlichting, Ilme1, 2, 3, 5, 8, 9, Autor           Weik, Martin, Autor mehr..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society, ou_1497692              
3Heme and Flavin Enzymes, Max Planck Institute for Medical Research, Max Planck Society, ou_1497715              
4Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society, ou_1497728              
5Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society, ou_1856341              
6Structural Biology of Elemental Cycles, Max Planck Institute for Medical Research, Max Planck Society, ou_2205646              
7Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society, ou_1497690              
8Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              
9Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Zusammenfassung: Reversibly switchable fluorescent proteins (RSFPs) serve as markers in advanced fluorescence imaging. Photoswitching from a non-fluorescent off-state to a fluorescent on-state involves trans-to-cis chromophore isomerization and proton transfer. Whereas excited-state events on the ps timescale have been structurally characterized, conformational changes on slower timescales remain elusive. Here we describe the off-to-on photoswitching mechanism in the RSFP rsEGFP2 by using a combination of time-resolved serial crystallography at an X-ray free-electron laser and ns-resolved pump–probe UV-visible spectroscopy. Ten ns after photoexcitation, the crystal structure features a chromophore that isomerized from trans to cis but the surrounding pocket features conformational differences compared to the final on-state. Spectroscopy identifies the chromophore in this ground-state photo-intermediate as being protonated. Deprotonation then occurs on the μs timescale and correlates with a conformational change of the conserved neighbouring histidine. Together with a previous excited-state study, our data allow establishing a detailed mechanism of off-to-on photoswitching in rsEGFP2.

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Sprache(n): eng - English
 Datum: 2018-05-282020-01-062020-02-062020-02
 Publikationsstatus: Erschienen
 Seiten: 11
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1038/s41467-020-14537-0
 Art des Abschluß: -

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Titel: Nature Communications
  Kurztitel : Nat. Commun.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: London : Nature Publishing Group
Seiten: - Band / Heft: 11 (741) Artikelnummer: 741 Start- / Endseite: 1 - 11 Identifikator: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723