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Spectra of intermediates in oxidation and reduction of cytochrome c oxidase ec

, : Spectra of intermediates in oxidation and reduction of cytochrome c oxidase ec Journal of Biological Chemistry 257(16): 9268-9270

Two kinetic components with distinct difference spectra occur during reduction of [bovine heart] cytochrome c oxidase by ruthenium hexamine. They are attributed to reduction of heme a (fast phase) and heme a3 (slow phase) (Scott and Gray (1980)). Two spectra seen during oxidation of cytochrome c oxidase by O2 were also attributed to oxidation of hemes a3 and a (Greenwood and Gibson (1967)). Spectra of the reductive and oxidative reactions obtained with the same preparations and the same apparatus under similar conditions are significantly different. The reactions appear to populate different reaction intermediates. Reconstitution into phospholipid vesicles do not affect these 2 spectra significantly. During turnover, the chief intermediates are those of the reductive pathway (Scott and Gray type intermediates). Reduction of heme a3 occurs .apprx. 70 times faster after turnover than the reduction of the resting enzyme. This is probably a dramatic pulsing effect.

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