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Bacteriorhodopsin: Structural Insights Revealed Using X-Ray Lasers and Synchrotron Radiation.

  • Wickstrand C Department of Chemistry and Molecular Biology, University of Gothenburg, SE-40530 Gothenburg, Sweden; email: richard.neutze@gu.se.
  • Nogly P Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.
  • Nango E RIKEN SPring-8 Center, Hyogo 679-5148, Japan.
  • Iwata S RIKEN SPring-8 Center, Hyogo 679-5148, Japan.
  • Standfuss J Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen, Switzerland.
  • Neutze R Department of Chemistry and Molecular Biology, University of Gothenburg, SE-40530 Gothenburg, Sweden; email: richard.neutze@gu.se.
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  • 2019-03-05
Published in:
  • Annual review of biochemistry. - 2019
X-ray free electron lasers
bacteriorhodopsin
bioenergetics
intermediate trapping
proton pumping
time-resolved serial femtosecond crystallography
Bacteriorhodopsins
Crystallography
Halobacterium salinarum
Ion Transport
Lasers
Models, Molecular
Protein Conformation
Protons
Retinaldehyde
Synchrotrons
X-Ray Diffraction
X-Rays
English Directional transport of protons across an energy transducing membrane-proton pumping-is ubiquitous in biology. Bacteriorhodopsin (bR) is a light-driven proton pump that is activated by a buried all-trans retinal chromophore being photoisomerized to a 13-cis conformation. The mechanism by which photoisomerization initiates directional proton transport against a proton concentration gradient has been studied by a myriad of biochemical, biophysical, and structural techniques. X-ray free electron lasers (XFELs) have created new opportunities to probe the structural dynamics of bR at room temperature on timescales from femtoseconds to milliseconds using time-resolved serial femtosecond crystallography (TR-SFX). Wereview these recent developments and highlight where XFEL studies reveal new details concerning the structural mechanism of retinal photoisomerization and proton pumping. We also discuss the extent to which these insights were anticipated by earlier intermediate trapping studies using synchrotron radiation. TR-SFX will open up the field for dynamical studies of other proteins that are not naturally light-sensitive.
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  • English
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green
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https://sonar.ch/global/documents/244450
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