Role of Hemoprotein P-450 in Fatty Acid ω-Hydroxylation in a Soluble Enzyme System from Liver Microsomes

Abstract

An enzyme system which catalyzes the ω-hydroxylation of fatty acids in the presence of reduced triphosphopyridine nucleotide and molecular oxygen has been obtained in a soluble form from rabbit liver microsomes. Three components have been separated from the microsomal extract and shown to be required for the conversion of laurate to ω-hydroxylaurate. These have been identified as hemoprotein P-450 (the carbon monoxide-binding pigment of microsomes), TPNH-cytochrome c reductase, and a heat-stable factor.