Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein
File(s) Schmidt_aad5081_combined_March2015_rev4_mesh.pdf (5.84 MB)
Accepted version
Author(s)
Type
Journal Article
Abstract
Many biological processes depend on detecting and responding to light. The response is often mediated by a structural change in a protein that begins when absorption of a photon causes isomerization of a chromophore bound to the protein. Pande et al. used x-ray pulses emitted by a free electron laser source to conduct time-resolved serial femtosecond crystallography in the time range of 100 fs to 3 ms. This allowed for the real-time tracking of the trans-cis isomerization of the chromophore in photoactive yellow protein and the associated structural changes in the protein.Science, this issue p. 725A 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.
Date Issued
2016-05-06
Date Acceptance
2016-04-05
Citation
Science, 2016, 352 (6286), pp.725-729
ISSN
1095-9203
Publisher
American Association for the Advancement of Science
Start Page
725
End Page
729
Journal / Book Title
Science
Volume
352
Issue
6286
Copyright Statement
© 2016 American Association for the Advancement of Science. All rights Reserved. This is the author’s version of the work. It is posted here by permission of the AAAS for personal
use, not for redistribution. The definitive version was published in Science, 06 May 2016,
Vol. 352, Issue 6286, pp. 725-729, DOI: 10.1126/science.aad5081
use, not for redistribution. The definitive version was published in Science, 06 May 2016,
Vol. 352, Issue 6286, pp. 725-729, DOI: 10.1126/science.aad5081
Sponsor
Engineering & Physical Science Research Council (EPSRC)
Identifier
https://science.sciencemag.org/content/352/6286/725/
Grant Number
EP/M000192/1
Subjects
Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
X-RAY-DIFFRACTION
TIME
CHROMOPHORE
PHOTOCYCLE
MYOGLOBIN
PHOTOISOMERIZATION
SPECTROSCOPY
EXCITATION
PATHWAYS
MOTIONS
Bacterial Proteins
Crystallography
Isomerism
Light
Photochemical Processes
Photons
Photoreceptors, Microbial
Protein Conformation
Time Factors
Bacterial Proteins
Photoreceptors, Microbial
Crystallography
Protein Conformation
Isomerism
Photons
Light
Time Factors
Photochemical Processes
General Science & Technology
Publication Status
Published
Date Publish Online
2016-05-06
