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Literature DB >> 3171

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

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.

Entities: Chemical Species

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Year: 1975 PMID： 3171 PMCID： PMC1172381 DOI： 10.1042/bj1510459

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

9 in total

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Journal: J Bacteriol Date: 1975-06 Impact factor: 3.490

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Authors: S I Kennedy; C A Fewson
Journal: Biochem J Date: 1968-04 Impact factor: 3.857

9 in total

16 in total

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Journal: Biochem J Date: 1979-01-01 Impact factor: 3.857

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Journal: Appl Environ Microbiol Date: 1998-05-01 Impact factor: 4.792

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