The Retinal Schiff Base-Counterion Complex of Bacteriorhodopsin: Changed Geometry during the Photocycle Is a Cause of Proton Transfer to Aspartate 85
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00206a001
Reference74 articles.
1. TIME-RESOLVED RESONANCE RAMAN STUDIES ON THE PHOTOCHEMICAL CYCLE OF BACTERIORHODOPSIN
2. The role of back-reactions and proton uptake during the N .fwdarw. O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study
3. Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle
4. ON THE MULTIPLE CYCLES OF BACTERIORHODOPSIN AT HIGH pH
5. Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle
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