| Home > Publications database > Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser |
| Journal Article | PUBDB-2018-05837 |
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2018
Moses King
Cambridge, Mass.
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Please use a persistent id in citations: doi:10.1126/science.aat0094 doi:10.3204/PUBDB-2018-05837
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.
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