[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-6.
STRAIN=Bath / NCIMB 11132;
DOI=10.1016/0378-1119(90)90158-N; PubMed=2205538 [NCBI, ExPASy, EBI, Israel, Japan]
Stainthorpe A.C.,
Lees V.,
Salmond G.P.C.,
Dalton H.,
Murrell J.C.;
"The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath).";
Gene 91:27-34(1990).
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[2]
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SEQUENCE REVISION TO 84; 306 AND 444.
McDonald I.,
Murrell J.C.;
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bath / NCIMB 11132;
DOI=10.1371/journal.pbio.0020303; PubMed=15383840 [NCBI, ExPASy, EBI, Israel, Japan]
Ward N.L.,
Larsen O.,
Sakwa J.,
Bruseth L.,
Khouri H.M.,
Durkin A.S.,
Dimitrov G.,
Jiang L.,
Scanlan D.,
Kang K.H.,
Lewis M.R.,
Nelson K.E.,
Methe B.A.,
Wu M.,
Heidelberg J.F.,
Paulsen I.T.,
Fouts D.E.,
Ravel J.,
Tettelin H., ![]()
Ren Q.,
Read T.D.,
DeBoy R.T.,
Seshadri R.,
Salzberg S.L.,
Jensen H.B.,
Birkeland N.K.,
Nelson W.C.,
Dodson R.J.,
Grindhaug S.H.,
Holt I.E.,
Eidhammer I.,
Jonasen I.,
Vanaken S.,
Utterback T.R.,
Feldblyum T.V.,
Fraser C.M.,
Lillehaug J.R.,
Eisen J.A.;
"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath).";
PLoS Biol. 2:1616-1628(2004).
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[4]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1038/366537a0; PubMed=8255292 [NCBI, ExPASy, EBI, Israel, Japan]
Rosenzweig A.C.,
Frederick C.A.,
Lippard S.J.,
Nordlund P.;
"Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.";
Nature 366:537-543(1993).
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[5]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1016/1074-5521(95)90222-8; PubMed=9432288 [NCBI, ExPASy, EBI, Israel, Japan]
Rosenzweig A.C.,
Nordlund P.,
Takahara P.M.,
Frederick C.A.,
Lippard S.J.;
"Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states.";
Chem. Biol. 2:409-418(1995).
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[6]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
STRAIN=Bath / NCIMB 11132;
DOI=10.1002/(SICI)1097-0134(199710)29:2<141::AID-PROT2>3.3.CO;2-W; PubMed=9329079 [NCBI, ExPASy, EBI, Israel, Japan]
Rosenzweig A.C.,
Brandstetter H.,
Whittington D.A.,
Nordlund P.,
Lippard S.J.,
Frederick C.A.;
"Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions.";
Proteins 29:141-152(1997).
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[7]
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X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
STRAIN=Bath / NCIMB 11132;
DOI=10.1021/ja003240n; PubMed=11456616 [NCBI, ExPASy, EBI, Israel, Japan]
Whittington D.A.,
Lippard S.J.;
"Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site.";
J. Am. Chem. Soc. 123:827-838(2001).
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- FUNCTION: Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.
- CATALYTIC ACTIVITY: Methane + NAD(P)H + O2 = methanol + NAD(P)+ + H2O.
- COFACTOR: Binds 2 iron ions.
- SUBUNIT: M.capsulatus has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane.
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