Peroxidase Activity of Mitochondrial Cytochrome c Oxidase

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T. V. Vygodina and A. A. Konstantinov^*

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-3181; E-mail: konst@genebee.msu.ru

^* To whom correspondence should be addressed.

Received May 23, 2007

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Mitochondrial cytochrome c oxidase is able to oxidize various aromatic compounds like o-dianisidine, benzidine and its derivatives (diaminobenzidine, etc.), p-phenylenediamine, as well as amidopyrine, melatonin, and some other pharmacologically and physiologically active substances via the peroxidase, but not the oxidase mechanism. Although specific peroxidase activity of cytochrome c oxidase is low compared with classical peroxidases, its activity may be of physiological or pathophysiological significance due to the presence of rather high concentrations of this enzyme in all tissues, as well as specific localization of the enzyme in the mitochondrial membrane favoring accumulation of hydrophobic aromatic substances.

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KEY WORDS: the oxygenase theory of A. N. Bach, respiratory chain, peroxidase activity, aromatic substrates

DOI: 10.1134/S0006297907100045

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