Mechanism of hydride transfer during the reduction of 3-acetylpyridine adenine dinucleotide by NADH catalyzed by the pyridine nucleotide transhydrogenase of Escherichia coli

FEBS Letters
P D Bragg

Abstract

The pyridine nucleotide transhydrogenase is a proton pump which catalyzes the reversible transfer of a hydride ion equivalent between NAD+ and NADP+ coupled to translocation of protons across the cytoplasmic membrane. The enzyme also catalyzes the reduction of the NAD+ analog 3-acetylpyridine adenine dinucleotide (AcPyAD+) by NADH. It has been proposed (Hutton et al. (1994) Eur. J. Biochem. 219, 1041-1051) that this reaction requires NADP(H) as an intermediate. Thus, NADP+ bound at the NADP(H)-binding site on the transhydrogenase would be reduced by NADH and reoxidized by AcPyAD+ binding alternately to the NAD(H)-binding site. The reduction of AcPyAD+ by NADPH would be a partial reaction in the reduction of AcPyAD+ by NADH. Using cytoplasmic membrane vesicles from mutants having elevated activities for transhydrogenation of AcPyAD+ by NADH in the absence of added NADP(H), the kinetics of reduction of AcPyAD+ by NADH and NADPH have been compared. The Km values for the reductants NADPH and NADH over a range of mutants, and for the non-mutant enzyme, differed to a much lesser degree than the Km for AcPyAD+ in the two reactions. The Km(AcPyAD) values for the transhydrogenation of AcPyAD+ by NADH were over an order of magnitude grea...Continue Reading

References

Oct 1, 1991·Journal of Bioenergetics and Biomembranes·J B Jackson
Aug 15, 1995·Biochimica Et Biophysica Acta·T OlaussonJ Rydström

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Citations

Oct 31, 2008·Journal of Bioenergetics and Biomembranes·Anders PedersenJan Rydström
Dec 1, 2011·The Journal of Physical Chemistry. B·Samrat DuttaChristopher M Cheatum

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