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Optical difference spectroscopy of liver mitochondria has revealed the presence of a cytochrome P450 species by its ligand reactions with carbon monoxide, metyrapone and diethylphenylphosphine. Its concentration of 0.15 nmol/mg mitochondrial protein is high enough to be detectable by ESR also. A microsomal contamination of the mitochondria could be excluded. Mitochondrial cytochrome P450 forms an enzyme-substrate complex with 5beta-cholestane-3alpha, 7alpha, 12alpha-triol with Ks value very similar to the Km value of the 26-hydroxylation of this substrate. This supports the existence in liver mitochondria of a cytochrome P450-dependent 26-monooxygenase for bile acid precursors, as previously postulated by us on the basis of a photochemical action spectrum.

Spectral Evidence for a Liver Mitochondrial Cytochrome P450 Involved in Bile Acid Metabolism