PMID: 9186780May 16, 1997Paper

The reduction of acetylpyridine adenine dinucleotide by NADH: is it a significant reaction of proton-translocating transhydrogenase, or an artefact?

Biochimica Et Biophysica Acta
S N StilwellJ B Jackson

Abstract

Transhydrogenase is a proton pump. It has separate binding sites for NAD+/NADH (on domain I of the protein) and for NADP+/NADPH (on domain III). Purified, detergent-dispersed transhydrogenase from Escherichia coli catalyses the reduction of the NAD+ analogue, acetylpyridine adenine dinucleotide (AcPdAD+), by NADH at a slow rate in the absence of added NADP+ or NADPH. Although it is slow, this reaction is surprising, since transhydrogenase is generally thought to catalyse hydride transfer between NAD(H)--or its analogues and NADP(H)--or its analogues, by a ternary complex mechanism. It is shown that hydride transfer occurs between the 4A position on the nicotinamide ring of NADH and the 4A position of AcPdAD+. On the basis of the known stereospecificity of the enzyme, this eliminates the possibilities of transhydrogenation(a) from NADH in domain I to AcPdAD+ wrongly located in domain III; and (b) from NADH wrongly located in domain III to AcPdAD+ in domain I. In the presence of low concentrations of added NADP+ or NADPH, detergent-dispersed E. coli transhydrogenase catalyses the very rapid reduction of AcPdAD+ by NADH. This reaction is cyclic; it takes place via the alternate oxidation of NADPH by AcPdAD+ and the reduction of NA...Continue Reading

Citations

Oct 31, 2008·Journal of Bioenergetics and Biomembranes·Anders PedersenJan Rydström
Oct 24, 2007·International Journal of Food Microbiology·Silvia A Dominguez, Donald W Schaffner
Aug 25, 2010·Biochimica Et Biophysica Acta·Lucinda HuxleyJ Baz Jackson
Apr 28, 2012·Biochimica Et Biophysica Acta·J Baz Jackson
Jun 10, 2009·Biochimica Et Biophysica Acta·Simon J WhiteheadJ Baz Jackson

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