Article
Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it.
Biophysical journal - 1 Feb 1997
Govindjee R, Imasheva E S, Misra S, Balashov S P, Ebrey T G, Chen N, Menick D R, Crouch R K
Abstract excerpt
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, the pKa of D85...
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