Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1979 Jan 1;177(1):361–364. doi: 10.1042/bj1770361

A comparison of the substrate and electron-donor specificities of the methane mono-oxygenases from three strains of methane-oxidizing bacteria.

D I Stirling, J Colby, H Dalton
PMCID: PMC1186376  PMID: 106847

Abstract

1. Methane mono-oxygenase from Methylosinus trichosporium has the same broad substrate specificity as the analogous enzyme from Methylococcus capsulatus (Bath); the enzyme from Methylomonas methanica is more specific. 2. Contrary to previous reports, NAD(P)H and not ascorbate is the required electron donor for the enzyme from Methylosinus trichosporium. 3. It is concluded that these three bacteria contain similar methane mono-oxygenases.

Full text

PDF
361

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Colby J., Dalton H. Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein. Biochem J. 1978 May 1;171(2):461–468. doi: 10.1042/bj1710461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Colby J., Dalton H. Some properties of a soluble methane mono-oxygenase from Methylococcus capsulatus strain Bath. Biochem J. 1976 Aug 1;157(2):495–497. doi: 10.1042/bj1570495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Colby J., Dalton H., Whittenbury R. An improved assay for bacterial methane mono-oxygenase: some properties of the enzyme from Methylomonas methanica. Biochem J. 1975 Nov;151(2):459–462. doi: 10.1042/bj1510459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Colby J., Stirling D. I., Dalton H. The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds. Biochem J. 1977 Aug 1;165(2):395–402. doi: 10.1042/bj1650395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ferenci T., Strom T., Quayle J. R. Oxidation of carbon monoxide and methane by Pseudomonas methanica. J Gen Microbiol. 1975 Nov;91(1):79–91. doi: 10.1099/00221287-91-1-79. [DOI] [PubMed] [Google Scholar]
  6. Salanitro J. P., Muirhead P. A. Quantitative method for the gas chromatographic analysis of short-chain monocarboxylic and dicarboxylic acids in fermentation media. Appl Microbiol. 1975 Mar;29(3):374–381. doi: 10.1128/am.29.3.374-381.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Stirling D. I., Dalton H. Effect of metal-binding and other compounds on methane oxidation by two strains of Methylococcus capsulatus. Arch Microbiol. 1977 Jul 26;114(1):71–76. doi: 10.1007/BF00429633. [DOI] [PubMed] [Google Scholar]
  8. Tonge G. M., Harrison D. E., Higgins I. J. Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b. Biochem J. 1977 Feb 1;161(2):333–344. doi: 10.1042/bj1610333. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES