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methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
1,1,1-trifluoropropane + reduced acceptor + H+ + O2
(2R)-1,1,1-trifluoropropan-2-ol + (2S)-1,1,1-trifluoropropan-2-ol + acceptor + H2O
-
-
the S stereoisomer is the dominant product
-
?
1-butene + reduced acceptor + H+ + O2
1,2-epoxybutane + acceptor + H2O
-
-
-
-
?
2 1-butene + 2 reduced acceptor + 2 H+ + 2 O2
3-buten-2-ol + 1,2-epoxybutane + 2 acceptor + 2 H2O
-
-
-
-
?
2 butane + 2 reduced acceptor + 2 H+ + 2 O2
1-butanol + 2-butanol + 2 acceptor + 2 H2O
-
-
-
-
?
2 pentane + 2 reduced acceptor + 2 H+ + 2 O2
1-pentanol + 2-pentanol + 2 acceptor + 2 H2O
-
-
-
-
?
2 propane + 2 reduced acceptor + 2 H+ + 2 O2
1-propanol + 2-propanol + 2 acceptor + 2 H2O
-
-
-
-
?
3 cis-2-butene + reduced acceptor + H+ + O2
meso-2,3-dimethyloxirane + acceptor + H2O
-
-
-
-
?
3,3,3-trifluoroprop-1-ene + reduced acceptor + H+ + O2
(2S)-2-(trifluoromethyl)oxirane + (2R)-2-(trifluoromethyl)oxirane + acceptor + H2O
-
-
the S stereoisomer is the dominant product
-
?
3,3,3-trifluoropropene + reduced acceptor + H+ + O2
3,3,3-trifluoro-1,2-epoxypropane + acceptor + H2O
-
-
-
-
?
cis-but-2-ene + reduced acceptor + H+ + O2
cis-2,3-dimethyloxirane + acceptor + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
methane + succinate + O2
methanol + fumarate + H2O
membrane-bound enzyme only
-
-
?
n-butane + reduced acceptor + O2
2-butanol + acceptor + H2O
-
-
-
?
n-pentane + reduced acceptor + O2
2-pentanol + acceptor + H2O
-
-
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
propylene + 2,3-dimethylquinol + O2
propylene oxide + 2,3-dimethylquinone + H2O
-
-
-
-
?
propylene + coenzyme Q0 + O2
propylene oxide + reduced coenzyme Q0 + H2O
-
-
-
-
?
propylene + decyl-plastoquinol + O2
propylene oxide + decyl-plastoquinone + H2O
-
higher activity compared to duroquinol
-
-
?
propylene + decylubiquinol + O2
propylene oxide + decylubiquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene epoxide + duroquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
-
-
-
-
?
propylene + menaquinol + O2
propylene oxide + menaquinone + H2O
-
-
-
-
?
propylene + trimethylquinol + O2
propylene oxide + trimethylquinone + H2O
-
-
-
-
?
trans-2-butene + reduced acceptor + H+ + O2
2,3-dimethyloxirane + acceptor + H2O
-
-
-
-
?
trans-but-2-ene + reduced acceptor + H+ + O2
(2R,3R)-trans-2,3-dimethyloxirane + (2S,3S)-trans-2,3-dimethyloxirane + acceptor + H2O
-
-
the S,S stereoisomer is the dominant product
-
?
additional information
?
-
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
Methylococcus capsulatus (Bath) is a methanotroph that possesses both a membrane-embedded (pMMO) and a soluble methane monooxygenase (sMMO). Major changes takes place in the respiratory chain between pMMO- and sMMO-producing cells. Quinones are predominantly used as the electron donors for methane oxidation by pMMO. During production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation
-
-
?
methane + quinol + O2
methanol + quinone + H2O
enzyme pMMO activity is dependent on oxygen concentrations
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
671965, 672301, 674005, 675831, 684112, 684114, 685113, 686085, 687284, 701759, 702501, 703343, 706752 -
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
Mn2+ + H2O2
?
-
-
-
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
-
-
-
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
-
enzyme form sMMO
-
?
additional information
?
-
-
unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
-
-
?
additional information
?
-
-
pMMO cannot oxidize naphthalene
-
-
?
additional information
?
-
-
pMMO has narrower substrate specificity but higher activity with smaller hydrocarbons like methane, ethane, and propene compared to sMMO
-
-
?
additional information
?
-
-
quinols are effective reductants for the detergent-solubilized enzyme, whereas NADH is ineffective
-
-
?
additional information
?
-
-
activity assays on membrane-bound pMMO routinely utilize NADH, succinate, or duroquinol as reductant, while only duroquinol and to a lesser extent, other quinols, are effective for solubilized and purified samples
-
-
?
additional information
?
-
activity assays on membrane-bound pMMO routinely utilize NADH, succinate, or duroquinol as reductant, while only duroquinol and to a lesser extent, other quinols, are effective for solubilized and purified samples
-
-
?
additional information
?
-
membrane-bound pMMO can efficiently oxidize straight-chain hydrocarbons from C1 to C5 with high regiospecificity and unusual stereoselectivity. Acetylene is a suicide substrate/inhibitor, the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit, there is a thermodynamic driving force for a ketene formed at the catalytic site to find its way to the water-exposed domain of subunit PmoB for acetylation, residue K196 of subunit PmoC that is acetylated, overview
-
-
?
additional information
?
-
methane oxidation activity of apo membrane-bound Methylococcus capsulatus (Bath) pMMO after metal loading using two copper reconstitution methods, overview
-
-
?
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Co2+
-
the enzyme contains three Co2+ ions per enzyme molecule
Fe
-
pMMOH bears a binuclear iron valence site [Fe(III)-Fe(IV)]
copper
-
contains both mononuclear copper and a copper-containing cluster. Each 200000 Da pMMO complex contains 4.8 copper ions. The purified particulate methane monooxygenase is a mixture of Cu(I) and Cu(II) oxidation states
copper
-
regulates the metabolic switch between the methane monooxygenase and the methane monooxygenase-NADH:quinone oxidoreductase complex, also regulates the level of expression of the pMMO and the development of internal membranes
copper
-
the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme. The copper ion interacts with three or four nitrogenic ligands, EPR-active copper
copper
-
required, activates
copper
contains 20.8 copper ions per 100 kDa protomer
copper
-
the enzyme contains 13 copper ions
copper
-
the enzyme contains a dicopper center
copper
the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron
Cu+
-
pMMO, requirement for, contains 12-15 Cu+ ions per molecule of enzyme
Cu+
-
the C-terminal domain of PmoB in pMMO is a reservoir for Cu(I) with properties similar to those of the E-cluster copper ions in the intact holoenzyme
Cu2+
-
required for activity
Cu2+
-
14.5 atoms per molecule of enzyme pMMO, type II copper centre
Cu2+
-
stimulation by methanobactin-Cu2+ complex, no activation in absence of methanobactin
Cu2+
-
the enzyme contains a mononuclear copper center and a dinuclear copper center, Cu-Cu interaction occurs in all redox forms of the enzyme, usage of mixed-valent dinuclear Cu model compounds, [tris{(N'-tert-butylureaylato)-N-ethyl}aminatocopper(II)]2BF4, and [N-tert-butylurealylato-{2-(dimethylamino)ethyl}aminatocopper(II)]2BF4, which are blue, and purple samples of [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-OTf)(THF)2], and [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-O2CCF3)(THF)2], EXAFS and Fourier transformation analysis, detailed interaction analysis, overview
Cu2+
-
contains a mononuclear and a dinculear Cu2+ center in the soluble domain of the 47 kDa subunit
Cu2+
-
Cu2+ is involved in the active site of pMMOH
Cu2+
-
multicopper enzyme, contains 3 Cu2+ ions per trimer, contains 13.6 copper atoms per protein complex
Cu2+
-
pMH contains 2-4 atoms of copper per a minimum molecular weight of 99 kDa
Cu2+
-
multi-copper enzyme with 14.1 copper atoms per protein, highest specific activity is observed wit 0.04 mM Cu2+ in the growth medium
Cu2+
-
pMMO contains a dicopper center and a mononuclear copper center, As-isolated enzyme conatins 10.2 Cu2+ equivalents per 100 kDa pMMO
Cu2+
-
the active enzyme contains approximately 15 copper atoms per mol
Cu2+
-
the enzyme is stimulated by exogenous copper (348% activity at 0.4 mM)
Cu2+
absolutely required, quantum refinement does not support dinuclear copper sites in crystal structures of particulate methane monooxygenase, copper content and binding structure analysis, crystal structures analysis from PDB IDs 3RGB and 3RFR, and modeling, QM-refined structures, detailed overview. Putative mechanism for the reaction of the mononuclear site with methane
Cu2+
an integral membrane metalloenzyme, the enzyme has a dicopper active site, structures of the dicopper site of enzyme pMMO, overview. Possible peroxo state of the dicopper site of pMMO from combined quantum mechanics and molecular mechanics calculations. The pMMO active site is considered to contain two Cu ions with a Cu-Cu distance of about 2.58 A within the pmoB subunit. One copper is coordinated by two histidine imidazoles, and another is chelated by a histidine imidazole and primary amine of an N-terminal histidine. The QM region contains the two Cu ions, His33, His137, His139, Tyr374, and Glu35 for the resting state, and, in addition, two oxygen atoms for the peroxo state
Cu2+
required for activity, each of pmoA, pmoB, and pmoC houses a dicopper center
Cu2+
required for activity, enzyme pMMO has a copper active site. Subdomain with a Cu-Cu distance of about 2.5 A, ligated by the N-terminal amino group and side chain of His33 (Cu1) as well as His137 and His139 (Cu2), and a zinc ion in PmoC about 20 A away from the PmoB dicopper site and attributed to the crystallization solution
Cu2+
required, preferred metal ion
Cu2+
the dicopper site is located at the N-terminus of the pmoB subunit, and conserved residues His33, His137, and His139 coordinate the copper ions. Copper center modeling: the first site is modeled as a single copper ion coordinated by residues His48 and His72 and is not present in other pMMOs. The second site, located near the membrane interface, is coordinated by residues His33, His137, and His139 and is highly conserved among pMMOs and related enzymes. The EPR measurements indicate that the dicopper site in pMMO contains one Cu(I) ion and one Cu(II) ion, proposed as a valence-localized mixed-valence Cu(I)Cu(II) pair, and that the monocopper site is present as Cu(I). The 1H ENDOR measurements show that the Cu(II) is not coordinated by a HxO ligand, so the two ions of the Cu(I)Cu(II) pair cannot be bridged by a hydroxo group in the as-isolated samples. The measurements do not rule out an oxo bridge
Cu2+
the enzyme complex contains multiple copper ions, 12-15 copper ions per protein monomer
Cu2+
two metal sites: a dicopper centre coordinated by histidine residues in subunit-B and a variable-metal site coordinated by carboxylate and histidine residues from subunit-C. A metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity
Fe2+
-
the enzyme contains one Fe2+ ion per enzyme molecule
Fe2+
-
As-isolated enzyme conatins 1.31 Fe2+ equivalents per 100 kDa pMMO
Fe2+
-
the active enzyme contains 2 iron atoms per mol
Fe3+
-
presence of an octahedral environment that may well be exchange-coupled to another paramagnetic species
Fe3+
-
contains a diiron(III) center
Iron
-
2.5 atoms per enzyme molecule of pMMO
Iron
-
each 200000 Da pMMO complex contains 1.5 iron ions
Iron
-
the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme, contains EPR-silent iron
Iron
-
pMH contains 1 or 2 atoms of nonheme iron
Zn2+
-
pMMO
Zn2+
-
the enzyme contains a nonphysiological mononuclear zinc center
Zn2+
-
contains one Zn2+ ion in the transmembrane domain
Zn2+
binds in the copper active site
Zn2+
can replace Cu2+, enzyme-bound, structure analysis, overview. Zinc binding at the pmoC site in the zinc-soaked structure stabilizes pmoC residues 200-210
Zn2+
one Zn2+ ion is bound per enzyme molecule
additional information
-
copper-induced iron-uptake
additional information
-
analysis of the oxidation states and coordination environments of the pMMO metal centers, overview
additional information
-
Zn2+ is not associated with purified pMMO
additional information
metal content of Methylococcus capsulatus (Bath) crude membranes before (as-isolated) and after (apo) cyanide treatment, and of apo-membranes after zinc and zinc/copper loading, overview. When zinc is loaded first, copper can replace one zinc site, which is likely the more accessible pmoC site. The activity of the zinc- and copper-loaded membrane-bound pMMO is 11-18% of the copper-reconstituted membrane-bound pMMO activity. This activity is lower than the 40-60% observed for copper- and zinc-loaded pMMO, even though the metal stoichiometries are similar, which is consistent with zinc occupying the active site when loaded first
additional information
the pMMO active site might possess a di-iron center located at the transmembrane zinc/copper site
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200000
-
non-denaturing PAGE
22000
-
1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
220000
-
purified pMMO-detergent complex, gel filtration
24000
-
1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
28376
-
1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
29063
-
1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
29073
-
1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry
29733
-
1 * 42785 + 1 * 29733 + 1 * 28328, MALDI-TOF mass spectrometry
300000
alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits
42786
-
1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
660000
-
solubilized enzyme, gel filtration
100000
about
23000
-
1 * 45000 + 1 * 26000 + 1 * 23000, pMMO, SDS-PAGE
23000
-
1 * 47000 + 1 * 26000 + 1 * 23000, three-dimensional structure analysis of purified pMMO by electron microscopy and single-particle analysis at 23 A resolution, overview
23000
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
23000
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
25000
-
1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
25000
-
1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH
25000
-
pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
26000
-
1 * 45000 + 1 * 26000 + 1 * 23000, pMMO, SDS-PAGE
26000
-
1 * 47000 + 1 * 26000 + 1 * 23000, three-dimensional structure analysis of purified pMMO by electron microscopy and single-particle analysis at 23 A resolution, overview
26000
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
27000
-
1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
27000
-
1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH
27000
-
pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
27000
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
28328
-
1 * 42785 + 1 * 29733 + 1 * 28328, MALDI-TOF mass spectrometry
28328
-
1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry
42785
-
1 * 42785 + 1 * 29733 + 1 * 28328, MALDI-TOF mass spectrometry
42785
-
1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry
45000
-
1 * 45000 + 1 * 26000 + 1 * 23000, pMMO, SDS-PAGE
45000
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
47000
-
1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
47000
-
1 * 47000 + 1 * 26000 + 1 * 23000, three-dimensional structure analysis of purified pMMO by electron microscopy and single-particle analysis at 23 A resolution, overview
47000
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
47000
-
1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
47000
-
1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH
47000
-
pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
99000
-
-
99000
-
pMMO, mass spectrometry
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Murrell, J.C.; Gilbert, B.; McDonald, I.R.
Molecular biology and regulation of methane monooxygenase
Arch. Microbiol.
173
325-332
2000
Methylococcus capsulatus, Methylococcus capsulatus Bath, Methylocystis sp., Methylomicrobium album, Methylomicrobium album BG8
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Zahn, J.A.; DiSpirito, A.A.
Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
J. Bacteriol.
178
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1996
Methylococcus capsulatus, Methylococcus capsulatus Bath
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The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization
J. Biol. Chem.
273
7957-7966
1998
Methylococcus capsulatus, Methylococcus capsulatus Bath
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Basu, P.; Katterle, B.; Andersson, K.K.; Dalton, H.
The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
Biochem. J.
369
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2003
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
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The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH:quinone oxidoreductase complex from Methylococcus capsulatus Bath
J. Bacteriol.
185
5755-5764
2003
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Lieberman, R.L.; Shrestha, D.B.; Doan, P.E.; Hoffman, B.M.; Stemmler, T.L.; Rosenzweig, A.C.
Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster
Proc. Natl. Acad. Sci. USA
100
3820-3825
2003
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Kitmitto, A.; Myronova, N.; Basu, P.; Dalton, H.
Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)
Biochemistry
44
10954-10965
2005
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Vasilev, V.I.; Tikhonova, T.V.; Gvozdev, R.I.; Tukhvatullin, I.A.; Popov, V.O.
Optimization of solubilization and purification procedures for the hydroxylase component of membrane-bound methane monooxygenase from Methylococcus capsulatus strain M
Biochemistry (Moscow)
71
1329-1335
2006
Methylococcus capsulatus, Methylococcus capsulatus M
brenda
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Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy
Inorg. Chem.
45
8372-8381
2006
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Choi, D.W.; Antholine, W.E.; Do, Y.S.; Semrau, J.D.; Kisting, C.J.; Kunz, R.C.; Campbell, D.; Rao, V.; Hartsel, S.C.; DiSpirito, A.A.
Effect of methanobactin on the activity and electron paramagnetic resonance spectra of the membrane-associated methane monooxygenase in Methylococcus capsulatus Bath
Microbiology
151
3417-3426
2005
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Balasubramanian, R.; Rosenzweig, A.C.
Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase
Acc. Chem. Res.
40
573-580
2007
Methylococcus capsulatus
brenda
Chan, S.I.; Yu, S.S.
Controlled oxidation of hydrocarbons by the membrane-bound methane monooxygenase: the case for a tricopper cluster
Acc. Chem. Res.
41
969-979
2008
Methylococcus capsulatus
brenda
Yu, S.S.; Ji, C.Z.; Wu, Y.P.; Lee, T.L.; Lai, C.H.; Lin, S.C.; Yang, Z.L.; Wang, V.C.; Chen, K.H.; Chan, S.I.
The C-terminal aqueous-exposed domain of the 45 kDa subunit of the particulate methane monooxygenase in Methylococcus capsulatus (Bath) is a Cu(I) sponge
Biochemistry
46
13762-13774
2007
Methylococcus capsulatus
brenda
Ng, K.Y.; Tu, L.C.; Wang, Y.S.; Chan, S.I.; Yu, S.S.
Probing the hydrophobic pocket of the active site in the particulate methane monooxygenase (pMMO) from Methylococcus capsulatus (Bath) by variable stereoselective alkane hydroxylation and olefin epoxidation
ChemBioChem
9
1116-1123
2008
Methylococcus capsulatus
brenda
Martinho, M.; Choi, D.W.; Dispirito, A.A.; Antholine, W.E.; Semrau, J.D.; Muenck, E.
Moessbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus Bath: evidence for a diiron center
J. Am. Chem. Soc.
129
15783-15785
2007
Methylococcus capsulatus
brenda
Tumanova, L.V.; Tukhvatullin, I.A.; Burbaev, D.S.; Gvozdev, R.I.; Andersson, K.K.
The binuclear iron site of membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M)
Russ. J. Bioorg. Chem.
34
177-185
2008
Methylococcus capsulatus, Methylococcus capsulatus M
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brenda
Zhang, Y.; Xin, J.; Chen, L.; Xia, C.
The methane monooxygenase intrinsic activity of kinds of methanotrophs
Appl. Biochem. Biotechnol.
157
431-441
2009
Methylococcus capsulatus, Methylococcus capsulatus HD6T, Methylomonas sp., Methylosinus trichosporium
brenda
Rosenzweig, A.C.
The metal centres of particulate methane mono-oxygenase
Biochem. Soc. Trans.
36
1134-1137
2008
Methylosinus trichosporium OB3b, Methylococcus capsulatus (G1UBD1), Methylococcus capsulatus, Methylococcus capsulatus Bath (G1UBD1)
brenda
Gvozdev, R.; Tukhvatullin, I.; Tumanova, L.
Purification and properties of membrane-bound methane hydroxylase from Methylococcus capsulatus (Strain M)
Biol. Bull.
35
161-169
2008
Methylococcus capsulatus, Methylococcus capsulatus M
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brenda
Himes, R.A.; Karlin, K.D.
Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO)
Curr. Opin. Chem. Biol.
13
119-131
2009
Methylococcus capsulatus, Methylococcus capsulatus Bath, Methylosinus trichosporium OB3b
brenda
Anthony, C.
A tribute to Howard Dalton and methane monooxygenase
Sci. Prog.
91
401-415
2008
Methylococcus capsulatus
brenda
Shiemke, A.K.; Cook, S.A.; Miley, T.; Singleton, P.
Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors
Arch. Biochem. Biophys.
321
421-428
1995
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Chan, S.I.; Nguyen, H.H.; Chen, K.H.; Yu, S.S.
Overexpression and purification of the particulate methane monooxygenase from Methylococcus capsulatus (Bath)
Methods Enzymol.
495
177-193
2011
Methylococcus capsulatus, Methylococcus capsulatus ATCC 33009
brenda
Smith, S.M.; Balasubramanian, R.; Rosenzweig, A.C.
Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit
Methods Enzymol.
495
195-210
2011
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Culpepper, M.A.; Rosenzweig, A.C.
Architecture and active site of particulate methane monooxygenase
Crit. Rev. Biochem. Mol. Biol.
47
483-492
2012
Methylocystis sp., Methylosinus trichosporium, Methylococcus capsulatus (Q607G3)
brenda
Culpepper, M.A.; Cutsail, G.E.; Hoffman, B.M.; Rosenzweig, A.C.
Evidence for oxygen binding at the active site of particulate methane monooxygenase
J. Am. Chem. Soc.
134
7640-7643
2012
Methylococcus capsulatus
brenda
Chen, K.H.; Wu, H.H.; Ke, S.F.; Rao, Y.T.; Tu, C.M.; Chen, Y.P.; Kuei, K.H.; Chen, Y.S.; Wang, V.C.; Kao, W.C.; Chan, S.I.
Bacteriohemerythrin bolsters the activity of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath)
J. Inorg. Biochem.
111
10-17
2012
Methylococcus capsulatus
brenda
Cao, L.; Caldararu, O.; Rosenzweig, A.C.; Ryde, U.
Quantum refinement does not support dinuclear copper sites in crystal structures of particulate methane monooxygenase
Angew. Chem. Int. Ed. Engl.
57
162 -166
2018
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3)
brenda
Culpepper, M.A.; Rosenzweig, A.C.
Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath)
Biochemistry
53
6211-6219
2014
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus, Methylococcus capsulatus Bath (G1UBD1 AND Q607G3)
brenda
Pham, M.D.; Lin, Y.P.; Van Vuong, Q.; Nagababu, P.; Chang, B.T.; Ng, K.Y.; Chen, C.H.; Han, C.C.; Chen, C.H.; Li, M.S.; Yu, S.S.; Chan, S.I.
Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene
Biochim. Biophys. Acta
1854
1842-1852
2015
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3)
brenda
Wang, V.C.; Maji, S.; Chen, P.P.; Lee, H.K.; Yu, S.S.; Chan, S.I.
Alkane oxidation methane monooxygenases, related enzymes, and their biomimetics
Chem. Rev.
117
8574-8621
2017
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3)
brenda
Itoyama, S.; Doitomi, K.; Kamachi, T.; Shiota, Y.; Yoshizawa, K.
Possible peroxo state of the dicopper site of particulate methane monooxygenase from combined quantum mechanics and molecular mechanics calculations
Inorg. Chem.
55
2771-2775
2016
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3)
brenda
Culpepper, M.A.; Cutsail, G.E.; Gunderson, W.A.; Hoffman, B.M.; Rosenzweig, A.C.
Identification of the valence and coordination environment of the particulate methane monooxygenase copper centers by advanced EPR characterization
J. Am. Chem. Soc.
136
11767-11775
2014
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3)
brenda
Sirajuddin, S.; Barupala, D.; Helling, S.; Marcus, K.; Stemmler, T.L.; Rosenzweig, A.C.
Effects of zinc on particulate methane monooxygenase activity and structure
J. Biol. Chem.
289
21782-21794
2014
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3), Methylocystis sp., Methylocystis sp. Rockwell
brenda
Ross, M.O.; Rosenzweig, A.C.
A tale of two methane monooxygenases
J. Biol. Inorg. Chem.
22
307-319
2017
Methylococcus capsulatus, Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath., Methylocystis sp., Methylocystis sp. M, Methylocystis sp. Rockwell, Methylosinus trichosporium
brenda
Liew, E.
Mutagenesis of the hydrocarbon monooxygenase indicates a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity
Microbiology
160
1267-1277
2014
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3), Methylocystis sp., Methylosinus trichosporium
brenda
Larsen, O.; Karlsen, O.A.
Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases
MicrobiologyOpen
5
254-267
2016
Methylococcus capsulatus, Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath.
brenda
Blanchette, C.D.; Knipe, J.M.; Stolaroff, J.K.; DeOtte, J.R.; Oakdale, J.S.; Maiti, A.; Lenhardt, J.M.; Sirajuddin, S.; Rosenzweig, A.C.; Baker, S.E.
Printable enzyme-embedded materials for methane to methanol conversion
Nat. Commun.
7
11900
2016
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3)
brenda
Zhang, S.; Karthikeyan, R.; Fernando, S.
Low-temperature biological activation of methane structure, function and molecular interactions of soluble and particulate methane monooxygenases
Rev. Environ. Sci. Biotechnol.
16
611-623
2017
Methylococcus capsulatus (G1UBD1 AND Q607G3), Methylococcus capsulatus Bath (G1UBD1 AND Q607G3), Methylocystis sp., Methylocystis sp. Rockwell, Methylosinus trichosporium
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brenda