title: Particulate methane monooxygenase from Methylosinus trichosporium OB3b.
abstract: Particulate methane monooxygenase (pMMO) catalyzes methane hydroxylation to methanol at ambient temperature and pressure. pMMO from Methylosinus trichosporium OB3b is one of the two pMMOs for which the protein structure was determined by X-ray crystallography. Because purified pMMO is inherently instable in vitro, it is difficult to use for time-consuming analysis. Therefore, investigations using crude enzyme preparations of pMMO are useful in some cases. In this chapter, methods for preparing pMMO from M. trichosporium OB3b to varying degrees of purity, including bacterial cells expressing pMMO, membrane fractions containing pMMO, and highly purified pMMO, are described.
authors.affiliation: Department of Environmental Chemistry and Engineering, Tokyo Institute of Technology, Nagatsuta-cho, Midori-ku, Yokohama, Japan.
authors.forename: Akimitsu
authors.initials: A
authors.lastname: Miyaji
mesh_terms: D000473:Alkanes / Q000378:metabolism; D000475:Alkenes / Q000378:metabolism; D002845:Chromatography / Q000379:methods; D018360:Crystallography, X-Ray; D003902:Detergents; D008670:Metals / Q000032:analysis; D000432:Methanol / Q000378:metabolism; D020602:Methylosinus trichosporium / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D012995:Solubility
chemical_list: D000473:Alkanes; D000475:Alkenes; D003902:Detergents; D008670:Metals; D010105:Oxygenases; C021555:methane monooxygenase; D000432:Methanol