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. 1975 Nov;151(2):459-62.
doi: 10.1042/bj1510459.

An improved assay for bacterial methane mono-oxygenase: some properties of the enzyme from Methylomonas methanica

J Colby, H Dalton, R Whittenbury

An improved assay for bacterial methane mono-oxygenase: some properties of the enzyme from Methylomonas methanica

J Colby et al. Biochem J. 1975 Nov.

Abstract

Extracts of Methylomonas methanica catalyse the O2-and NAD(P)H-dependent disappearance of bromomethane. The activity is unstable at 2 degrees C but is stable at --70 degrees C for several weeks. Bromomethane mono-oxygenase is particulate and is inhibited by metal-binding reagents, by compounds SKF 525A and Lilly 53325, by some metal ions and by acetylene. Evidence is presented that indicates that bromomethane mono-oxygenase is the enzyme responsible for methane oxidation in vivo.

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