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• W2050972133 endingPage "1055" @default.
• W2050972133 startingPage "1049" @default.
• W2050972133 abstract "Abstract— The photocycle of the proton pump bacteriorhodopsin contains two consecutive intermediates in which the retinal Schiff base is unprotonated; the reaction between these states, termed M 1 and M 2 , was suggested to be the switch in the proton transport which reorients the Schiff base from D85 on the extracellular side to D96 on the cytoplasmic side (Váró and Lanyi, Biochemistry 30 , 5016–5022, 1991). At pH 10 the absorption maxima of both M 1 and M 2 could be determined in the recombinant D96N protein. We find that M 1 absorbs at 411 nm as do M 1 and M 2 in wild‐type bacteriorhodopsin, but M 2 absorbs at 404 nm. Thus, in M, but not M 2 the unprotonated Schiff base is affected by the D96N residue replacement. The connectivity of the Schiff base to D96 in the detected M 2 state, but not in M 1 , is thereby established. On the other hand, the photostationary state which develops during illumination of D85N bacteriorhodopsin contains an M state corresponding to M 1 with an absorption maximum shifted to 400 nm, suggesting that this species in turn is affected by D85. These results are consistent with the suggestion that M 1 and M 2 are pre‐switch and post‐switch states, respectively." @default.
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• W2050972133 date "1992-12-01" @default.
• W2050972133 modified "2023-10-14" @default.
• W2050972133 title "THE TWO CONSECUTIVE M SUBSTATES IN THE PHOTOCYCLE OF BACTERIORHODOPSIN ARE AFFECTED SPECIFICALLY BY THE D85N AND D96N RESIDUE REPLACEMENTS" @default.
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• W2050972133 doi "https://doi.org/10.1111/j.1751-1097.1992.tb09728.x" @default.
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