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The proton-translocating nicotinamide adenine dinucleotide transhydrogenase

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Abstract

H+-transhydrogenase couples the reversible transfer of hydride ion equivalents between NAD(H) and NADP(H) to the translocation of protons across a membrane. There are separate sites on the enzyme for the binding of NAD(H) and of NADP(H). There are some indications of the position of the binding sites in the primary sequence of the enzymes from mitochondria andEscherichia coli. Transfer of hydride ion equivalents only proceeds when a reduced and an oxidized nucleotide are simultaneously bound to the enzyme. When Δp=0 the rate of interconversion of the ternary complexes of enzyme and nucleotide substrates is probably limiting. An increase in Δp accelerates the rate of interconversion in the direction of NADH → NADP+ until another kinetic component, possibly product release, becomes limiting. The available data are consistent with either direct or indirect mechanisms of energy coupling.

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Abbreviations

DCCD:

N N1-dicyclohexylcarbodiimide

FSBA:

51-[p-(fluorosulfonyl)benzoyl] adenosine

FCCP:

carbonylcyanide-p-fluoromethoxyphenylhydrazone

H+-Thase:

H+-transhydrogenase

thio-NADP+ :

thionicotinamide adenine dinucleotide phosphate

AcPdAd+ :

3-acetylpyridine adenine dinucleotide

Δp :

proton electrochemical gradient

Δψ:

membane potential

ΔpH:

pH difference across the membrane

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    J. B. Jackson

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Jackson, J.B. The proton-translocating nicotinamide adenine dinucleotide transhydrogenase. J Bioenerg Biomembr 23, 715–741 (1991). https://doi.org/10.1007/BF00785998

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