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Arg82 is one of the four buried charged residues in the retinal binding pocket of bacteriorhodopsin (bR). Previous studies show that Arg82 controls the pKas of Asp85 and the proton release group and is essential for fast light-induced proton release. To further investigate the role of Arg82 in light-induced proton pumping, we replaced Arg82 with histidine and studied the resulting pigment and its...
K129 is a residue located in the extracellular loop connecting transmembrane helices D and E of bacteriorhodopsin. Replacement of K129 with a histidine alters the pKa's of two key residues in the proton transport pathway, D85, and the proton release group (probably E204); the resulting pigment has properties that differ markedly from the wild type. 1) In the unphotolyzed state of the K129H mutant,...
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