|Gene:||mmoC||Accession Number: G-2930 (MetaCyc)|
Species: Methylosinus trichosporium OB3b
Component of: soluble methane monooxygenase (extended summary available)
The reductase component of the soluble methane monooxygenase (MMOR) is an iron-sulfur flavoprotein, whose main responsibility is to shuttle electrons from NADH through its FAD and [2Fe-2S] cofactors to the hydroxylase active site [Lund85, Lund85a].
Gene Citations: [Cardy91]
Molecular Weight of Polypeptide: 39.7 kD (experimental) [Fox89 ]
Relationship Links: Entrez-Nucleotide:RELATED-TO:X55394 , InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR001221 , InterPro:IN-FAMILY:IPR001433 , InterPro:IN-FAMILY:IPR001709 , InterPro:IN-FAMILY:IPR008333 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR017927 , InterPro:IN-FAMILY:IPR017938 , Pfam:IN-FAMILY:PF00111 , Pfam:IN-FAMILY:PF00175 , Pfam:IN-FAMILY:PF00970 , Prints:IN-FAMILY:PR00371 , Prints:IN-FAMILY:PR00410 , Prosite:IN-FAMILY:PS51384
|MultiFun Terms:||metabolism → carbon utilization → carbon compounds|
Subunit of: soluble methane monooxygenase
Species: Methylosinus trichosporium OB3b
Subunit composition of
soluble methane monooxygenase = [([MmoX][MmoY][MmoZ])2][MmoC][MmoB][OrfY]
soluble methane monooxygenase hydroxylase component dimer = ([MmoX][MmoY][MmoZ])2 (summary available)
soluble methane monooxygenase hydroxylase component monomer = (MmoX)(MmoY)(MmoZ)
soluble methane monooxygenase hydroxylase component α subunit = MmoX (summary available)
soluble methane monooxygenase hydroxylase component β subunit = MmoY (summary available)
soluble methane monooxygenase hydroxylase component γ subunit = MmoZ (summary available)
soluble methane monooxygenase reductase component = MmoC (summary available)
soluble methane monooxygenase regulatory component = MmoB (summary available)
soluble methane monooxygenase MMOD component = OrfY
Almost all methanotrophic bacteria contain a membrane-bound, copper-dependent, particulate form of MMO (pMMO), and some also express a soluble form (sMMO) under conditions of low copper availability. The sMMO proteins are more stable and easier to purify than those of pMMO, and the enzymes from Methylococcus capsulatus Bath and Methylosinus trichosporium OB3b in particular have been studied in considerable detail over the last decade.
Full catalytic activity requires the presence of three protein components. Reductive activation of dioxygen and the oxidation of methane occur at carboxylate-bridged diiron centers in the subunits of the hydroxylase enzyme MMOH, a 251-kDa α2β2γ2 protein. A reductase, MMOR, which contains both a [2Fe-2S] ferredoxin and an FAD (flavine adenine dinucleotide) domain, provides electrons to MMOH by oxidizing NADH to NAD+. Finally, the presence of a small cofactorless protein, MMOB, is required for efficient catalysis [Fox89].
Recent work demonstrated that a fourth protein, MMOD, is also involved in the sMMO system [Merkx02].
Three substrates are involved in the reaction of sMMO. Both O2 and CH4 react at the dinuclear iron centers of MMOH, whereas the third, NADH, reacts at the FAD center of MMOR. Steady-state kinetic data support a catalytic cycle in which the sMMO system reacts sequentially with CH4, NADH, and O2. Initially, methane binds to the oxidized hydroxylase. NADH subsequently transfers a hydride to the FAD moiety of MMOR, and two electrons are transmitted sequentially from the reduced FAD through the [2Fe-2S] center of MMOR to a binuclear non-heme iron cluster(III) center of the hydroxylase by means of intra- and intermolecular electron-transfer reactions. Molecular oxygen then binds to the diiron(II) center of the hydroxylase where it is reductively activated to hydroxylate methane, forming methanol and water [Gassner99].
Enzymatic reaction of: methane monooxygenase
EC Number: 220.127.116.11
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: methane oxidation to methanol I
Cofactors or Prosthetic Groups: binuclear non-heme iron cluster
Cardy91: Cardy DL, Laidler V, Salmond GP, Murrell JC (1991). "The methane monooxygenase gene cluster of Methylosinus trichosporium: cloning and sequencing of the mmoC gene." Arch Microbiol 156(6);477-83. PMID: 1785954
Fox89: Fox BG, Froland WA, Dege JE, Lipscomb JD (1989). "Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph." J Biol Chem 264(17);10023-33. PMID: 2542319
Lund85: Lund J, Dalton H (1985). "Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath)." Eur J Biochem 147(2);291-6. PMID: 2982614
Merkx02: Merkx M, Lippard SJ (2002). "Why OrfY? Characterization of MMOD, a long overlooked component of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)." J Biol Chem 277(8);5858-65. PMID: 11709550
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493