The methane monooxygenase gene cluster of Methylosinus trichosporium: cloning and sequencing of the mmoC gene
Archives of Microbiology, ISSN: 0302-8933, Vol: 156, Issue: 6, Page: 477-483
1991
- 38Citations
- 23Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations38
- Citation Indexes38
- 38
- CrossRef27
- Captures23
- Readers23
- 23
Article Description
Methane monooxygenase (MMO) is the enzyme responsible for the conversion of methane to methanol in methanotrophic bacteria. The soluble MMO enzyme complex from Methylosinus trichosporium also oxidizes a wide range of aliphatic and aromatic compounds in a number of potentially useful biotransformations. In this study we have used heterologous DNA probes from the type X methanotroph Methylococcus capsulatus (Bath) to isolate mmo genes from the type II methanotroph M. trichosporium. We report here that the gene encoding the reductase component, Protein C of MMO, lies adjacent to the genes encoding the other components of soluble MMO in M. trichosporium but is separated by an open reading frame of unknown function, orfY. The complete nucleotide sequence of these genes is presented. Sequence analysis of mmoC indicates that the N-terminus of Protein C has significant homology with 2Fe2S ferredoxins from a wide range of organisms. © 1991 Springer-Verlag.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0026044876&origin=inward; http://dx.doi.org/10.1007/bf00245395; http://www.ncbi.nlm.nih.gov/pubmed/1785954; http://link.springer.com/10.1007/BF00245395; https://dx.doi.org/10.1007/bf00245395; https://link.springer.com/article/10.1007/BF00245395
Springer Science and Business Media LLC
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