Soluble methane monooxygenase

Fox BG, Bomeman JG, Wackett LP, et al. 1990. Haloalkane oxidation by the soluble methane monooxygenase irom Methylosinus trichosporium OB3b Mechanistic and environmental implications. Biochemistry 29 6419-6427. 

Lipscomb ID (1994) Biochemistry of the soluble methane monooxygenase. Annu Rev Microbiol 48 371-399. 

Patel RN, CT Hou, Al Laskin, A Felix (1982) Microbial oxidation of hydrocarbons properties of a soluble methane monooxygenase from a facultative methane-utilizing organism, Methylobacterium sp. strain CRL-26. Appl Environ Microbiol 44 1130-1137. 

Oldenhuis R, RLJM Vink, DB Janssen, B Witholt (1989) Degradation of chlorinated aliphatic hydrocarbons by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase. Appl Environ... 

Jahng D, TK Wood (1994) Trichloroethylene and chloroform degradation by a recombinant pseudomonad expresssing soluble methane monooxygenase from Methylosinus trichosporium OB3b. Appl Environ Microbiol 60 2473-2482. 

STUDIES OF THE SOLUBLE METHANE MONOOXYGENASE PROTEIN SYSTEM STRUCTURE, COMPONENT INTERACTIONS, AND HYDROXYLATION MECHANISM... 

J. S. Lloyd, R. Finch, H. Dalton, J. C. Murrell (1999) Homologous expression of soluble methane monooxygenase genes in Methylosinus trichosporium OB3b. Microbiology, 145 461-470... 

Two types of methane monooxygenases have been studied (1) soluble methane monooxygenase (sMMO) and (2) particulate (membrane-bound) methane monooxygenase (pMMO). The well-studied sMMO is produced by methanotrophs under copper-limiting conditions. All methanotrophs produce pMMO—found in intracytoplasmic membranes— but it is the less well-studied enzyme. 

Solid-state supramolecular complexes, see Su-pramolecular copper(l)/silver(I) complexes Solubility products, 17 215 Soluble methane monooxygenase protein system, 42 263-286 hydroxylation... 

Studies of the Soluble Methane Monooxygenase Protein System Structure, Component Interactions, and Hydroxylation Mechanism Katherine E. Liu and Stephen J. Lippard... 

Colby, J., D. I. Stirling, and H. Dalton, The soluble methane monooxygenase from Methylococcus copsulatus bath - Its ability to oxygenate n-alkanes, ethers and alicyclic, aromatic, and heterocyclic compounds , Biochem. J., 165, 395-402 (1977). 

Koh, S.-C., J. P. Bowman, and G. S. Sayler, Soluble methane monooxygenase production and trichloroethylene degradation by a type I methanotroph, Methylomonas methanica 68-1 , Appl. Environ. Microbiol., 59,960-967 (1993). 

Phelps, P. A., Agarwal, S. K., Speitel, G. E., Jr Georgiou, G. (1992). Methylosinus trichosporium OB3b mutants having constitutive expression of soluble methane monooxygenase in the presence of high levels of copper. Applied and Environmental Microbiology, 58, 3701-8. 

Scheme 2.6 Examples of reactions catalyzed byenzymesthat carry a dinudear iron active site (a) hydroxylation of methane by soluble methane monooxygenase (sMMO) [7] (b) reduction of ribonucleotides by class I ribonucleotide reductase (RNR)...

Green, J. Dalton, H. Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity. J. Biol. Chem. 1985, 260(29), 15795-15801. 

G. T. Gassner and S. J. Lippard, Component interactions in the soluble methane monooxygenase system, Biochem. 38, 12768-12785 (1999). 

Tinberg CE, Lippard SJ. Dioxygen activation in soluble methane monooxygenase. Acc Chem Res. 2011 44 280-88. 

Jin, Y. and Lipscomb, J.D. (2000) Mechanistic insights C-H activation from radical clock chemistry oxidation of substituted methylcyclopropanes catalyzed by soluble methane monooxygenase from Methylosynus trichosporium OB3b, Biochim. Biophys. Acta 1543, 47-59. 

Kopp, D.A., Gassner, George T., Blazyk, J.L., and Lippard, S.J. (2001) Electron-transfer reactions of the reductase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath). 

Muller, J., Lugovskoy, A. A., Wagner, G., and Lippard, S.J. (2002) NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase. Biochemistry 41, 42-51. 

Stahl, S.S., Fransicsco, W. A., Merkx, M., Klinman, J.P., and Lippard, S.J. (2001) Oxygen kinetic isotope effects in soluble methane monooxygenase, J. Biol. Chem. 276,4549-4553. 

---