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Biochim Biophys Acta. 2012 Oct;1817(10):1879-85. doi: 10.1016/j.bbabio.2012.03.033. Epub 2012 Apr 5.

Mitochondrial hydrogen peroxide production as determined by the pyridine nucleotide pool and its redox state.

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1
Department of Biochemistry, Moscow State University, Moscow, Russian Federation.

Abstract

The rates of NADH-supported superoxide/hydrogen peroxide production by membrane-bound bovine heart respiratory complex I, soluble pig heart dihydrolipoamide dehydrogenase (DLDH), and by accompanying operation of these enzymes in rat heart mitochondrial matrix were measured as a function of the pool of pyridine nucleotides and its redox state. Each of the activities showed nontrivial dependence on nucleotide pool concentration. The NAD(+)/NADH ratios required for their half maximal capacities were determined. About half of the total NADH-supported H(2)O(2) production by permeabilized mitochondria in the absence of stimulating ammonium could be accounted for by DLDH activity. The significance of the mitochondrial NADH-dependent hydrogen peroxide production under physiologically relevant conditions is discussed. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012).

PMID:
22503830
DOI:
10.1016/j.bbabio.2012.03.033
[Indexed for MEDLINE]
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