The mitochondrial oxidation of quinol monophosphates

Author:

Young J. M.1

Affiliation:

1. School of Molecular Sciences, University of Warwick, Coventry CV4 7AL, U.K.

Abstract

1. Mitochondria from ox heart and rat liver catalysed a slow cyanide-sensitive oxidation of 2,3-dimethylnaphthaquinol monophosphate, duroquinol monophosphate, menadiol 1-phosphate and menadiol 4-phosphate. 2. The release of Pi was concomitant with oxygen uptake. 3. The oxidation was somewhat stimulated by Ca2+ and Pi, and weakly inhibited by 2,4-dinitrophenol. 4. The quinol monophosphates effected a rapid reduction of free cytochrome c, and consequently addition of cytochrome c greatly increased the rate of the mitochondrial oxidation of 2,3-dimethylnaphthaquinol monophosphate. 5. This quinol phosphate interacts with the electron-transport chain at the level of cytochrome c. 6. Polylysine promoted an interaction between 2,3-dimethylnaphthaquinol monophosphate and cytochrome oxidase. Thus, although polylysine blocks mitochondrial oxidations via reduced cytochrome c, the oxidation of the quinol phosphate was strongly stimulated. 7. This stimulation was most effective in the most intact mitochondrial preparations and was inhibited by ADP and by Pi. 8. The implications of these results for factors limiting the rate of quinol phosphate oxidation, the mode of action of stimulators and the mechanism of Pi formation are discussed.

Publisher

Portland Press Ltd.

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