SOME PROPERTIES OF THE CYTOCHROME OXIDASE OF PENICILLIUM CHRYSOGENUM

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Abstract
P. chrvsogenum contained a pigment with an absorption spectrum closely resembling that of mammalian cytochrome c; cell-free preparations of this organism were capable of oxidizing this pigment as well as oxidizing and reducing mammalian cytochrome c. The oxidation of cytochrome c by extracts was inhibited by CO to the same extent as the respiration on whole cells. No absorption maximum was noted in the region characteristic for cytochrome c oxidase. The cytochrome c oxidase of this organism was inhibited by cyanide, azide, hydroxylamine, and CO but the inhibition by CO was not reversed by light. Among the metal complexing agents, only o-phenathroline caused inhibition of the oxidase. Phosphate and a certain ionic strength were essential for maximum activity of the oxidase and the product of oxidation was water. The suggestion is made that the cytochrome c oxidase of P. chrysogenum is not a typical hematin enzyme.

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