Methane monooxygenase (particulate)

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Methane monooxygenase (particulate)
1yew.jpg
Particulate methane monooxygenase hexa-heterotrimer, Methylococcus capsulatus
Identifiers
EC number1.14.18.3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Methane monooxygenase (particulate) (EC 1.14.18.3) is an enzyme with systematic name methane,quinol:oxygen oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction

methane + quinol + O2 methanol + quinone + H2O

Methane monooxygenase contains copper. It is membrane-bound.

References[edit]

  1. ^ Shiemke, A.K.; Cook, S.A.; Miley, T.; Singleton, P. (1995). "Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors". Arch. Biochem. Biophys. 321 (2): 421–428. doi:10.1006/abbi.1995.1413. PMID 7646068.
  2. ^ Basu, P.; Katterle, B.; Andersson, K.K.; Dalton, H. (2003). "The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein". Biochem. J. 369 (Pt 2): 417–427. doi:10.1042/BJ20020823. PMC 1223091. PMID 12379148.
  3. ^ Kitmitto, A.; Myronova, N.; Basu, P.; Dalton, H. (2005). "Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)". Biochemistry. 44 (33): 10954–10965. doi:10.1021/bi050820u. PMID 16101279.
  4. ^ Balasubramanian, R.; Rosenzweig, A.C. (2007). "Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase". Acc. Chem. Res. 40 (7): 573–580. doi:10.1021/ar700004s. PMID 17444606.

See also[edit]

External links[edit]