Carbon monoxide and hydroxymercuribenzoate sensitivity of a fatty acid (ω-2) hydroxylase from Bacillus megaterium

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Summary

A soluble monooxygenase system from Bacillus megaterium, which hydroxlates fatty acids primarily in the (ω-2) position in the presence of NADPH and 02, is 50% inhibited by carbon monoxide at a CO:02 ratio of 0.25 and 85% inhibited by 5 μM p-hydroxymercuribenzoate. The latter inhibition can be reversed by ferredoxin, cysteine or glutathione. These data are interpreted as indicating the involvement of a P-450-type cytochrome and a ferredoxin-type component in the hydroxylation. This system is not inhibited by superoxide dismutase, catalase or by moderate concentrations of various hydroxyl radical scavengers.

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