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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.
Peterson et al. (Tue,) studied this question.