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• W2055366828 abstract "In mitochondria and bacteria, transhydrogenase uses the transmembrane proton gradient (δp) to drive reduction of NADP+ by NADH. We have investigated the pre-steady-state kinetics of NADP+ reduction by acetylpyridine adenine dinucleotide (AcPdADH, an analogue of NADH) in complexes formed from the two, separately prepared, recombinant, peripheral subunits of the enzyme: the dI component, which binds NAD+ and NADH, and the dIII component, which binds NADP+ and NADPH. In the stopped-flow spectrophotometer the reaction proceeds as a single-turnover burst of hydride transfer to NADP+ on dIII before product NADPH release becomes limiting in steady state. The burst is biphasic. The results indicate that the fast phase represents direct hydride transfer from AcPdADH to NADP+ in dI:dIII complexes, and that the slow phase, which predominates when [dI] &lt; [dIII], corresponds to dissociation of the protein complexes during multiple turnovers of dI. Measurements on the amplitude of the burst, and on the apparent first-order rate constant of the fast phase, indicate that the equilibrium constant of the hydride-transfer step on the enzyme is shifted relative to that in solution. This has consequences for a model proposed earlier, in which δp is used, not at the hydride-transfer step, but to change the binding affinities of NADP+ and NADPH." @default.
• W2055366828 created "2016-06-24" @default.
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• W2055366828 date "1999-07-08" @default.
• W2055366828 modified "2023-09-25" @default.
• W2055366828 title "A shift in the equilibrium constant at the catalytic site of proton-translocating transhydrogenase: significance for a ‘binding-change’ mechanism" @default.
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• W2055366828 doi "https://doi.org/10.1042/bj3410329" @default.
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