The dihydrocozymase-cytochrome c reductase activity of heart-muscle preparation

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Abstract
The Co I H2, cytochrome c reductase activity of heart-muscle preparation was about the same as its succinate-cytochrome c reductase activity at room temp. The concn. of oxidized cytochrome c did not fall exponentially with time during the course of the reduction. The rate of reduction of cytochrome c was approx. a rectangular hyperbolic function of the oxidized cytochrome c concn. The rate of reduction of the endogenous cytochrome c of the heart-muscle prepn., calculated from the rate of the aerobic oxidation of Co I H2, was 1200 times that of the same concn. of cytochrome c added to the heart-muscle prepn. The Co I H2-cytochrome c reductase activity of heart-muscle prepn. was inactivated by treatment with BAL. It was concluded that the Co I H2-cytochrome c reductase in heart-muscle prepn. consisted of 2 or more enzymes.