The Enzyme Database

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EC 1.14.18.3     
Accepted name: methane monooxygenase (particulate)
Reaction: methane + quinol + O2 = methanol + quinone + H2O
Systematic name: methane,quinol:oxygen oxidoreductase
Comments: Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shiemke, A.K., Cook, S.A., Miley, T. and Singleton, P. Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors. Arch. Biochem. Biophys. 321 (1995) 421–428. [PMID: 7646068]
2.  Basu, P., Katterle, B., Andersson, K.K. and Dalton, H. The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 369 (2003) 417–427. [PMID: 12379148]
3.  Kitmitto, A., Myronova, N., Basu, P. and Dalton, H. Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath). Biochemistry 44 (2005) 10954–10965. [PMID: 16101279]
4.  Balasubramanian, R. and Rosenzweig, A.C. Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase. Acc. Chem. Res. 40 (2007) 573–580. [PMID: 17444606]
[EC 1.14.18.3 created 2011]
 
 


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