The proton-translocating nicotinamide adenine dinucleotide transhydrogenase

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 and Escherichia coli. Transfer of hydride ion equivalents only proceeds when a reduced and an oxidized nucleotide are simultaneously bound to the enzyme. When delta p = 0 the rate of interconversion of the ternary complexes of enzyme and nucleotide substrates is probably limiting. An increase in delta p 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.