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

The Biochemical journal ·Vol. 151 ·No. 2 ·1975-11-00 ·Pages 459-62

Colby J, Dalton H, Whittenbury R

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.

MeSH Terms

Hydrogen-Ion Concentration Methane Methylococcaceae/enzymology Oxygenases/analysis,antagonists & inhibitors Proadifen Temperature

Chemicals

Proadifen Oxygenases bromomethane mono-oxygenase Methane

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Colby J

Dalton H

Whittenbury R

References (9)

9 references, click to expand

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The binding of metyrapone to cytochrome P-450 and its inhibitory action on microsomal hepatic mixed function oxidation reactions.
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Enzymes of the mandelate pathway in Bacterium N.C.I.B. 8250.
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FEBS Lett. 1970 Nov 9;11(1):41-44 PMID: 11945445

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1510459

Published

1975-11-00

Pages

459-62

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1172381

Subset

External Links

PubMed source DOI: 10.1042/bj1510459 PMC Full Text View journal details

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

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