Abstract
A procedure to extract directly from mitochondrial membranes cytochrome oxidase as a protein lipid complex into hexane and ethyl ether in a functional state is described. Upon evaporation of the solvent, the residue can be used to form liposomes that display cytochrome oxidase activity. This activity can be inhibited in the liposomes and in the mitochondrial membranes by dicyclohexylcarbodiimide and triphenyltin chloride, provided a high inhibitor/cytochrome oxidase ratio is employed. It would appear that the binding of one mol of dicyclohexylcarbodiimide chloride oxidase inhibits proton translocation, whilst the binding of at least two mol inhibits electron transport.
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