Methane monooxygenase (particulate)

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Methane monooxygenase (particulate)
Particulate methane monooxygenase hexa-heterotrimer, Methylococcus capsulatus
EC no.
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Methane monooxygenase (particulate) (EC 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 enzyme present in methanotrophs.

See also[edit]


  1. ^ Shiemke AK, Cook SA, Miley T, Singleton P (August 1995). "Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors". Archives of Biochemistry and Biophysics. 321 (2): 421–8. doi:10.1006/abbi.1995.1413. PMID 7646068.
  2. ^ Basu P, Katterle B, Andersson KK, Dalton H (January 2003). "The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein". The Biochemical Journal. 369 (Pt 2): 417–27. doi:10.1042/BJ20020823. PMC 1223091. PMID 12379148.
  3. ^ Kitmitto A, Myronova N, Basu P, Dalton H (August 2005). "Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)". Biochemistry. 44 (33): 10954–65. doi:10.1021/bi050820u. PMID 16101279.
  4. ^ Balasubramanian R, Rosenzweig AC (July 2007). "Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase". Accounts of Chemical Research. 40 (7): 573–80. doi:10.1021/ar700004s. PMID 17444606.

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