Cardy D L, Laidler V, Salmond G P, Murrell J C
Department of Biological Sciences, University of Warwick, Coventry, UK.
Arch Microbiol. 1991;156(6):477-83. doi: 10.1007/BF00245395.
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.
甲烷单加氧酶（MMO）是负责在甲烷营养细菌中将甲烷转化为甲醇的酶。来自 trichosporium甲基弯曲菌的可溶性MMO酶复合物还能在一些潜在有用的生物转化过程中氧化多种脂肪族和芳香族化合物。在本研究中，我们使用来自X型甲烷营养菌巴氏甲基球菌的异源DNA探针，从II型甲烷营养菌trichosporium甲基弯曲菌中分离出mmo基因。我们在此报告，编码MMO还原酶组分（蛋白C）的基因，在trichosporium甲基弯曲菌中与编码可溶性MMO其他组分的基因相邻，但被一个功能未知的开放阅读框orfY隔开。文中给出了这些基因的完整核苷酸序列。mmoC的序列分析表明，蛋白C的N端与来自多种生物的2Fe2S铁氧化还原蛋白具有显著同源性。
