Methylococcus capsulatus, methane

Methylococcus capsulatus, methane monooxygenase, diferric iron cluster, 43 362-363 2-(l-Methylpyridinium-4-yl)-4,4,5,5,-... 

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. 

Sessions, A. L., Jahnke, L. L., Schimmelmann, A. and Hayes, J. M. (2002) Hydrogen isotope fractionation in lipids of the methane oxidizing bacterium Methylococcus capsulatus. Geochimica et Cosmochimica Acta 66, 3955. 

T. Hanczar, L. Bodrossy, R. Csaki, J.C. Murrell, K. L. Kovacs (2002) Hydrogen driven methane oxidation in Methylococcus capsulatus (Bath). Arch. Microbiol., 177 167-172... 

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... 

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. 

The multiprotein complex methane monooxygenase (MMO) serves meth-anotrophs to convert methane to methanol. It can be either soluble (sMMO) or membrane bound ( particulate , pMMO) and it typically consists of three components, a reductase (MMOR), a component termed protein B (MMOB) and a hydroxylase denoted MMOH. The nature of the metal cofactors in the latter component are reasonably well understood for sMMO as will be discussed in the non-heme iron section. For the pMMO of Methylococcus capsulatus an obligate requirement for copper was shown. As reported in reference 1 a trinuclear Cu(II) cluster was discussed128 but the number and coordination of coppers still is a matter of continuing investigation since then. 

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. 

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. 

Willems, J-P., Valentine, A.M., Gurbiel, R., Lippard, S.J., and Hoffman, B.M. (1998) Small molecule binding to the mixed-valent diiron center of methane monooxygenase hydroxylase from Methylococcus capsulatus... 

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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