Komrakov AYu

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The photocycles of the wild-type bacteriorhodopsin and the D96N mutant were investigated by the flash-photolysis technique. The M-intermediate formation (400 nm) and the L-intermediate decay (520 nm) were found to be well described by a sum of two exponents (time constants, tau 1 = 65 and tau 2 = 250 microseconds) for the wild-type bR and three exponents(More)
The hypothesis on the additional function of the ATP/ADP antiporter (ANT) as uncoupling protein has been tested in proteoliposomes and planar bilayer phospholipid membranes (BLM). It is found that dissipation of the light-induced delta pH in the dark is very much faster in ANT-bacteriorhodopsin proteoliposomes than in proteoliposomes containing(More)
In our previous work [(1993) FEBS Lett. 313, 248-250; (1993) Biochem. Int. 30, 461-469] M-intermediate formation of wild-type bacteriorhodopsin was shown to involve two components differing in time constants (tau 1 = 60-70 microseconds and tau 2 = 220-250 microseconds), which were suggested to reflect two independent pathways of M-intermediate formation.(More)
The flash-photolysis technique was used to study the photocycles of the wild-type bacteriorhodopsin (WT bR) and D96N mutant. Kinetics of the L-intermediate decay and M-intermediate formation at pH 7.0, 20 degrees C fit well a sum of two components having time constants, tau (1) = 60 microS and tau (2) = 250 microS, for the WT bR, and a sum of three(More)
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