Abstract
Cytochrome c oxidase is the terminal enzyme in electron transport. It catalyzes the transfer of four electrons from cytochrome c and four protons of unknown origin to dioxygen, which is converted into two molecules of water. (For a thorough review see Wikstrom et al., 1981). Mammalian cytochrome oxidase is a large Y-shaped molecule that spans the inner mitochondrial membrane (Deatherage et al., 1983; Kim et al., 1985), and consists of one copy of each of 1–13 subunits (Kadenbach et al., 1986; Kuhn-Nentwig and Kadenbach, 1985 & 1986; Buse et al., 1985; Capaldi and Zhang, 1986). The enzyme has two functional domains: cytochrome a, which contains one heme (aFe) and one copper (CuA); and cytochrome a3, which contains the remaining herae (a3Fe) and copper (CuB). Cytochrome a3 is the site of ligand binding and dioxygen reduction.
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Fiamingo, F.G., Altschuld, R.A., Alben, J.O. (1988). Multiple Forms of Cytochrome C Oxidase Observed in Heart Tissue, Myocytes, and Mitochondria by Fourier Transform Infrared Spectroscopy. In: Lemasters, J.J., Hackenbrock, C.R., Thurman, R.G., Westerhoff, H.V. (eds) Integration of Mitochondrial Function. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2551-0_8
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