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Enzymatic ohgr-Oxidation

I. ELECTRON CARRIERS IN FATTY ACID AND HYDROCARBON HYDROXYLATION

Julian A. Peterson 1, Debkumar Basu 1, and Minor J. Coon 1

From the 1 From the Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104

The separation of the soluble ohgr-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 ohgr-hydroxylase. All three proteins are required for the conversion of laurate to ohgr-hydroxylaurate or of octane to n-octanol in the presence of Fe++ ions, reduced diphosphopyridine nucleotide, and molecular oxygen.

Submitted on August 18, 1966


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