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Methanotrophic Methylococcus capsulatus

R. L. Csaki. Bodrossy, T. Hanczar, J. C. Murrell, K. L. Kovacs (2001) Molecular characterization of a membrane bound hydrogenase in the methanotroph Methylococcus capsulatus (Bath). FEMSMicrobiol. Lett., 205 203-207... [Pg.30]

Copper enzymes are involved in reactions with a large number of other, mostly inorganic substrates. In addition to its role in oxygen and superoxide activation described above, copper is also involved in enzymes that activate methane, nitrite and nitrous oxide. The structure of particulate methane mono-oxygenase from the methanotrophic bacteria Methylococcus capsulatus has been determined at a resolution of 2.8 A. It is a trimer with an a3P33 polypeptide arrangement. Two metal centres, modelled as mononuclear and dinuclear copper, are located in the soluble part of each P-subunit, which resembles CcOx subunit II. A third metal centre, occupied by Zn in the crystal, is located within the membrane. [Pg.251]

Similar forms of sMMO are expressed by morphologically and meta-bolically distinct methanotrophs that have been classified as Type X and Type II (Lipscomb, 1994). These are typified by Methylococcus capsulatus Bath (MMO Bath) and Methylosinus trichosporium OB3b (MMO OB3b), respectively. The parallel studies of sMMO from these two organisms has facilitated the description of both the essential features of the enzyme... [Pg.234]

See other pages where Methanotrophic Methylococcus capsulatus is mentioned: [Pg.323]    [Pg.323]    [Pg.13]    [Pg.24]    [Pg.139]    [Pg.309]    [Pg.478]    [Pg.165]    [Pg.165]    [Pg.137]    [Pg.413]    [Pg.254]    [Pg.311]    [Pg.375]    [Pg.285]    [Pg.285]    [Pg.65]   
See also in sourсe #XX -- [ Pg.323 , Pg.328 , Pg.330 ]



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Methanotroph

Methanotrophes

Methylococcus

Methylococcus capsulatus

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