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Two groups control light-induced schiff base deprotonation and the proton affinity of asp(85) in the Arg(82)His mutant of bacteriorhodopsin

Arg(82) is one of the four buried charged residues in the retinal binding pocket of bacteriorhodopsin (bR). Previous studies show that Arg(82) controls the pK(a)s of Asp(85) and the proton release group and is essential for fast light-induced proton release. To further investigate the role of Arg(82...

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Библиографические подробности
Главные авторы: Imasheva, ES, Balashov, SP, Ebrey, TG, Chen, N, Crouch, RK, Menick, DR
Формат: Artigo
Язык:Inglês
Опубликовано: 1999
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC1300548/
https://ncbi.nlm.nih.gov/pubmed/10545374
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