Methylococcus capsulatus Bath

The soluble MMO from Methylococcus capsulatus (Bath) is able to oxidize chloro- and bromomethane—but not iodomethane—with the presumptive formation of formaldehyde (Colby et al. 1977). 

Colby J, DI Stirling, H Dalton (1977) The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate -alkanes, -alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds. Biochem J 165 395-401. 

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... 

H. H. T. Nguyen, S. J. Elliott, J. H. K. Yip, S. I. Chan (1998) The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme - Isolation and characterization. J. Biol. Chem., 273 7957-7966... 

S. H. Stanley, H. Dalton (1992) The biotransformation of propylene to propylene oxide by Methylococcus capsulatus (Bath) 1. Optimization of rates. Biocatalysis, 6 163-175... 

The presence or absence of Ca + ions in one or both sites also appears to effect the reduction potential of the high-potential heme. In equilibrium redox titrations monitored spectroscopically, done in the presence of Ca + ions, this is shifted positive by about 50 mV PP = - - 226 mV) compared with titrations done in the presence of a chelator (IP = -1-176 mV) (52). This former value is close to the reduction potentials reported for the high-potential heme in the CCP from P. aeruginosa (51), but about 200 mV lower than reported for the high-potential hemes in the enzymes from N. europea (46) and Methylococcus capsulatus Bath (80). In contrast, the reduction potential of the peroxidatic heme is unaffected by the presence or absence of Ca + ions (16, 52). 

It seems probable that other redox centres contain this binuclear iron structure, but that this has not yet been recognized. For example, a non-heme iron protein of the methane monooxygenase from Methylococcus capsulatus (Bath), which functions as the oxygenase in equation (28), has been described as having a novel iron centre which is not an iron-sulfur cluster. This may well be an oxo-bridged system. Analysis suggests 2.3 Fe per molecule of protein. 

Basu, P. Katterle, B. Andersson, K. K. Dalton, H. The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 2003, 369(2), 417 127. 

Lieberman, R. L. Shrestha, D. B. Doan, P. E. Hoffman, B. M. Stemmier, T. L. Rosenzweig, A. C. Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster. Proc. Natl. Acad. Sci. USA 2003, 100(1), 3820-3825. 

Zahn, J. A. DiSpirito, A. A. Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J. Bacteriol. 1996, 178(4), 1018-1029. 

Martinho, M. Choi, D. W. Dispirito, A. A. Antholine, W. E. Semrau, J. D. Miinck, E. Mossbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus bath evidence for a diiron center. J. Am. Chem. Soc. 2007, 729(51), 15783-15785. 

Kitmitto, A. Myronova, N. Basu, R Dalton, H. Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath). Biochemistry 2005, 44(33), 10954-10965. 

The crystallographic structures of MMOH from both microorganisms, Methylococcus capsulatus (Bath) and Methylosynus trichosporium OB3b have been... 

Gassner, G.T., Lippard, S.J. (1999) Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). Biochemistry 38, 12768-12785. 

Liu, K.E., Valentine, A.M., Wang, D., Huynh, B.H. Edmondson, D.E. Salifoglou, A. Lippard, SJ. (1995) Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath), J. Am. Chem. Soc. 117, 10174-10185. 

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... 

Davydov, R., Valentine, A. M., Komar-Panicucci, S., Hoffman, B. M., and Lippard, S. J., 1999, An EPR study of the dinuclear iron site in the soluble methane monooxygenase from Methylococcus capsulatus (Bath) reduced by one electron at 77K the effects of component interactions and the binding of small molecules to the diiron(lll) center. Biochemistry 38 418864197. 

Green, J., and Dalton, H., 1989, A stopped-flow kinetic study of the soluble methane monooxygenase from Methylococcus capsulatus (Bath), Biochem J. 259 167nl72. 

Liu, K. E., and Lippard, S. J., 1991, Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath). Effects of protein B, reductase, and subsh ate [published erratum appears in J. Biol. Chem. 1991, 266 24859], J. Biol. Chem. 266 12836nl2839. 

Nguyen, H. H., Nakagawa, K. H., Hedman, B., Elliott, S. J., Lidstrom, M. E., Hodgson, K. O., and Chan, S. L, 1996, X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxygenase from Methylococcus capsulatus (Bath)6 Cu(I) Ions and their implications, J. Am. Chem. Soc. 118 12766nl2776. 

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