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Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

  • Kanupriya Pande
  • , Christopher D.M. Hutchison
  • , Gerrit Groenhof
  • , Andy Aquila
  • , Josef S. Robinson
  • , Jason Tenboer
  • , Shibom Basu
  • , Sébastien Boutet
  • , Daniel P. DePonte
  • , Mengning Liang
  • , Thomas A. White
  • , Nadia A. Zatsepin
  • , Oleksandr Yefanov
  • , Dmitry Morozov
  • , Dominik Oberthuer
  • , Cornelius Gati
  • , Ganesh Subramanian
  • , Daniel James
  • , Yun Zhao
  • , Jake Koralek
  • Jennifer Brayshaw, Christopher Kupitz, Chelsie Conrad, Shatabdi Roy-Chowdhury, Jesse D. Coe, Markus Metz, Paulraj Lourdu Xavier, Thomas D. Grant, Jason E. Koglin, Gihan Ketawala, Raimund Fromme, Vukica Srajer, Robert Henning, John C. Spence, Abbas Ourmazd, Peter Schwander, Uwe Weierstall, Matthias Frank, Petra Fromme, Anton Barty, Henry N. Chapman, Keith Moffat, Jasper J. Van Thor, Marius Schmidt
  • University of Wisconsin-Milwaukee
  • German Electron Synchrotron
  • Imperial College London
  • University of Jyväskylä
  • SLAC National Accelerator Laboratory
  • Arizona State University
  • Max-Planck Institute for the Structure and Dynamics of Matter
  • The University of Chicago
  • Lawrence Livermore National Laboratory
  • University of Hamburg

Research output: Contribution to journalArticlepeer-review

381 Scopus citations

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.

Original languageEnglish
Pages (from-to)725-729
Number of pages5
JournalScience
Volume352
Issue number6286
DOIs
StatePublished - May 6 2016

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