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The reaction of cytochrome oxidase with carbon monoxide.

E. Ball,C. F. Strittmatter,O. Cooper

Published 1951 in Journal of Biological Chemistry

ABSTRACT

The participation of molecular oxygen in biological oxidations is catalyzed by an enzyme which has been called-a variety of names starting with Atmungsfemzent by Warburg (18) to the currently employed term of cytochrome oxidase proposed by Keilin and Hartree (11). Presumably the enzyme functions by first combining with molecular oxygen and then becoming oxidized by it. As first shown by Warburg (19), the enzyme is poisoned by carbon monoxide which competes with oxygen for the reduced form of the enzyme. Data in the,literature on the quantitative aspects of this competition are sparse and in poor agreement. We present here additional data on this point. The reaction of the enzyme with carbon monoxide has been the chief means of characterizing it. Warburg and Negelein (22) by an indirect method obtained the absorption spectrum of the carbon monoxide complex of the enzyme and so obtained evidence that the enzyme was an iron porph yrin compound. However, the positive identification of cytochrome oxidase itself with any of the hemochromogen bands to be seen in living tissue or its extracts has not been unequivocally achieved. We present here results obtained by direct quantitative spectroscopic measurements that bear on the nature of cytochrome oxidase and its combination with carbon monoxide.

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