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Membr Cell Biol. 1998;12(5):743-54.

Photoreactivation of the cytochrome oxidase complex with cyanide: the reaction of heme a3 photoreduction.

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  • 1Institute of Photobiology, Belarus National Academy of Sciences, Minsk.

Abstract

Electron transfer activity of isolated cytochrome oxidase inhibited by low concentrations of cyanide by 93-95% was shown to rise no less than three times under exposure to visible light. Irradiation with visible light was found to increase the rate of reduction of cytochrome oxidase heme groups in the presence of sodium dithionite. Based on these results, it is suggested that the modification of the catalytic and spectral characteristic of the cytochrome oxidase-cyanide complex is due to the photostimulation of the intramolecular electron transport at the interheme (heme a heme a3) transfer stage, i.e., is caused by photoreduction of the enzyme's heme a3-CN complex.

PMID:
10379650
[PubMed - indexed for MEDLINE]
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