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• W1965560171 abstract "The functions of the four aspartic acid residues in interhelical loops at the cytoplasmic surface of bacteriorhodopsin, Asp-36, Asp-38, Asp-102, and Asp-104, were investigated by studying single and multiple aspartic acid to asparagine mutants. The same mutants were examined also with the additional D96N residue replacement. The kinetics of the M and N intermediates of the photochemical cycles of these recombinant proteins were affected only in a minor, although self-consistent, way. When residue 38 is an aspartate and anionic, it makes the internal proton exchange between the retinal Schiff base and Asp-96 about 3 times more rapid, and events associated with the reisomerization of retinal to all-trans about 3 times slower. Asp-36 has the opposite effect on these processes, but to a smaller extent. Asp-102 and Asp-104 have even less or none of these effects. Of the four aspartates, only Asp-36 could play a direct role in proton uptake at the cytoplasmic surface. In the 13 bacterioopsin sequences now available, only this surface aspartate is conserved." @default.
• W1965560171 created "2016-06-24" @default.
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• W1965560171 date "1999-04-30" @default.
• W1965560171 modified "2023-09-27" @default.
• W1965560171 title "Functional Roles of Aspartic Acid Residues at the Cytoplasmic Surface of Bacteriorhodopsin" @default.
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• W1965560171 doi "https://doi.org/10.1021/bi990101d" @default.
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