Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin

Bacteriorhodopsin (bR) is a light-driven proton pump. Here the authors combine time-resolved crystallography at a free-electron laser, ultrafast spectroscopy and quantum chemistry to study the structural changes following multiphoton photoexcitation of bR and find that they occur within 300 fs not o...

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Autores principales: Gabriela Nass Kovacs, Jacques-Philippe Colletier, Marie Luise Grünbein, Yang Yang, Till Stensitzki, Alexander Batyuk, Sergio Carbajo, R. Bruce Doak, David Ehrenberg, Lutz Foucar, Raphael Gasper, Alexander Gorel, Mario Hilpert, Marco Kloos, Jason E. Koglin, Jochen Reinstein, Christopher M. Roome, Ramona Schlesinger, Matthew Seaberg, Robert L. Shoeman, Miriam Stricker, Sébastien Boutet, Stefan Haacke, Joachim Heberle, Karsten Heyne, Tatiana Domratcheva, Thomas R. M. Barends, Ilme Schlichting
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/a086ef8dd24c43efbb5f1448e1c960cf
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Sumario:Bacteriorhodopsin (bR) is a light-driven proton pump. Here the authors combine time-resolved crystallography at a free-electron laser, ultrafast spectroscopy and quantum chemistry to study the structural changes following multiphoton photoexcitation of bR and find that they occur within 300 fs not only in the light-absorbing chromophore but also in the surrounding protein.