Enzymatic ω-Oxidation

Abstract

Abstract The separation of the soluble ω-hydroxylation system of Pseudomonas oleovorans into three components is reported in this paper. They have been identified as rubredoxin (a red protein containing nonheme iron but no inorganic sulfide), a diphosphopyridine nucleotide-rubredoxin reductase, and the ω-hydroxylase. All three proteins are required for the conversion of laurate to ω-hydroxylaurate or of octane to n-octanol in the presence of Fe++ ions, reduced diphosphopyridine nucleotide, and molecular oxygen.