Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00059a015
Reference72 articles.
1. The role of back-reactions and proton uptake during the N .fwdarw. O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study
2. Energy storage in the primary step of the photocycle of bacteriorhodopsin
3. Revised assignment of energy storage in the primary photochemical event in bacteriorhodopsin
4. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M—-N transition
5. Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct.
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