Oxidation of ferrocytochrome C by chicken heart mitochondria cytochrome C oxidase

Cytochrome c oxidase from a number if eukaryotic organisms have been isolated and thoroughly investigated in various laboratories. Chicken cytochrome c oxidase from heart mitochondria was isolated and study was conducted in view of its structural and functional properties. Spectral properties of chicken oxidase were found to be similar to that of bovin oxidase as standared. Both oxidase posses Cu and Fe atoms. Sedimentation equilibrium [S] values indicated chicken heart cytochrome C oxidase as 9+5s and beef oxidase as 11 S in dimeric form at physiological pH. Polypeptide composition of monomers and dimmers are identical