Cytochrome Oxidase

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Abstract
Using Na des-oxycholate to dissolve the oxidase complex, in the prepn. of cytochrome oxidase, a material was obtained which, when tested with the hydroquinone-cytochrome c system at pH 7.4, was 2.5 times as active as the Keilin and Hartree oxidase prepn. It retained its activity after centrifugation for 2 hrs. at 18,000 X g. or after having been passed through a Seitz filter. Both prepns. were clear and red-brown. Partial purification was achieved by fractionating with Na desoxy- cholate, and the final prepn. was 4-6 times as active as the original parent Keilin and Hartree oxidase. The Na des-oxycholate prepns. were unable to mediate the oxidation of d-glucose by d-glucose dehydrogenase of mammalian liver, even though diphosphopyridine nucleotide and cytochrome c were added. Cytochrome oxidase should be a constituent of these Na desoxycholate-Keilin and Hartree oxidase prepns. This conclusion was based on the inhibitory action of NaCN and NaN3, and on the fact that the O2 consumption was reduced about 95% in the absence of cytochrome c.

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