Methane monooxygenase (particulate)

Methane monooxygenase (particulate)
Identifiers
EC number 1.14.18.3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB 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 \rightleftharpoons methanol + quinone + H2O

Methane monooxygenase contains copper. It is membrane-bound.

References

  1. ↑ Shiemke, A.K., Cook, S.A., Miley, T. and 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. and 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. and 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. and 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

External links

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.