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• W2078013419 abstract "At high ionic strength, the pH dependence of the M intermediate decay in a photocycle of the D96N mutant bacteriorhodopsin shows a complicated behavior which is found to be due to the coexistence of two pathways of the M conversion. The M decay which dominates at pH <5 is coupled to the proton uptake from the cytoplasmic surface and proceeds probably through the N intermediate. This pathway is inhibited by glutaraldehyde, the potent inhibitor of M decay in the wildtype bacteriorhodopsin and of the azide‐facilitated M decay in the D96N mutant. Another pathway of the M decay is predominant at pH > 5. This pathway is insensitive to glutaraldehyde and some other similar inhibitors (lutetium ions, sucrose and glycerol). On the other hand, it is sensitive to the pK changes of the group X (Glu‐204) in the outward proton pathway. Possibly, the M decay through this pathway represents a reverse H + transport process (the proton uptake from the external surface) and proceeds via the L intermediate." @default.
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• W2078013419 date "1996-12-16" @default.
• W2078013419 modified "2023-09-26" @default.
• W2078013419 title "Complicated character of the M decay pH dependence in the D96N mutant is due to the two pathways of the M conversion" @default.
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• W2078013419 doi "https://doi.org/10.1016/s0014-5793(96)01334-8" @default.
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