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The methane monooxygenase gene cluster ofMethylosinus trichosporium: cloning and sequencing of themmoC gene

✍ Scribed by D. L. N. Cardy; V. Laidler; G. P. C. Salmond; J. C. Murrell

Publisher
Springer
Year
1991
Tongue
English
Weight
680 KB
Volume
156
Category
Article
ISSN
0302-8933

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✦ Synopsis

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.

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