Journal Article PUBDB-2018-05837

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Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser

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2018
Moses King Cambridge, Mass.

Science 361(6398), eaat0094 () [10.1126/science.aat0094]
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Abstract: Ultrafast isomerization of retinal is the primary step in photoresponsive biological functions including vision in humans and ion transport across bacterial membranes. We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin. A series of structural snapshots with near-atomic spatial resolution and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket before passing through a twisted geometry and emerging in the 13-cis conformation. Our findings suggest ultrafast collective motions of aspartic acid residues and functional water molecules in the proximity of the retinal Schiff base as a key facet of this stereoselective and efficient photochemical reaction.

Classification:

Note: © The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science

Contributing Institute(s):
  1. FS-CFEL-1 (Group Leader: Henry Chapman) (CFEL-I)
  2. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)
Research Program(s):
  1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
Experiment(s):
  1. Measurement at external facility

Appears in the scientific report 2018
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 Record created 2018-12-20, last modified 2025-07-29


Published on 2018-07-13. Available in OpenAccess from 2019-01-13.:
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