| Literature DB >> 27151871 |
Kanupriya Pande1, Christopher D M Hutchison2, Gerrit Groenhof3, Andy Aquila4, Josef S Robinson4, Jason Tenboer5, Shibom Basu6, Sébastien Boutet4, Daniel P DePonte4, Mengning Liang4, Thomas A White7, Nadia A Zatsepin8, Oleksandr Yefanov7, Dmitry Morozov3, Dominik Oberthuer7, Cornelius Gati7, Ganesh Subramanian8, Daniel James8, Yun Zhao8, Jake Koralek4, Jennifer Brayshaw5, Christopher Kupitz5, Chelsie Conrad6, Shatabdi Roy-Chowdhury6, Jesse D Coe6, Markus Metz7, Paulraj Lourdu Xavier9, Thomas D Grant10, Jason E Koglin4, Gihan Ketawala6, Raimund Fromme6, Vukica Šrajer11, Robert Henning11, John C H Spence8, Abbas Ourmazd5, Peter Schwander5, Uwe Weierstall8, Matthias Frank12, Petra Fromme6, Anton Barty7, Henry N Chapman13, Keith Moffat14, Jasper J van Thor2, Marius Schmidt5.
Abstract
A variety of organisms have evolved mechanisms to detect and respond to light, in which the response is mediated by protein structural changes after photon absorption. The initial step is often the photoisomerization of a conjugated chromophore. Isomerization occurs on ultrafast time scales and is substantially influenced by the chromophore environment. Here we identify structural changes associated with the earliest steps in the trans-to-cis isomerization of the chromophore in photoactive yellow protein. Femtosecond hard x-ray pulses emitted by the Linac Coherent Light Source were used to conduct time-resolved serial femtosecond crystallography on photoactive yellow protein microcrystals over a time range from 100 femtoseconds to 3 picoseconds to determine the structural dynamics of the photoisomerization reaction.Entities:
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Year: 2016 PMID： 27151871 PMCID： PMC5291079 DOI： 10.1126/science.aad5081
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728