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Information on EC 1.14.18.3 - methane monooxygenase (particulate) and Organism(s) Methylococcus capsulatus and UniProt Accession G1UBD1

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IUBMB Comments
Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25).
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Methylococcus capsulatus
UNIPROT: G1UBD1
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Word Map
The taxonomic range for the selected organisms is: Methylococcus capsulatus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
particulate mmo, spmob, membrane-bound methane monooxygenase, membrane-associated methane monooxygenase, particulate methane mono-oxygenase, pmmo hydroxylase, pmmo2, particulate methane monooxygenase a, pmmo1, copper-containing membrane monooxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
particulate methane mono-oxygenase
-
copper-containing membrane monooxygenase
-
membrane-associated methane monooxygenase
-
-
membrane-bound methane monooxygenase
membrane-embedded methane monooxygenase
-
methane hydroxylase
-
-
particulate methane monooxygenase
particulate methane-oxidizing complex
-
-
pMMO hydroxylase
-
-
PmoB
-
large subunit of pMMO
spmoB
-
recombinant soluble domains of the pmoB subunit of particulate methane monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methane + quinol + O2 = methanol + quinone + H2O
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
methane,quinol:oxygen oxidoreductase
Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
show the reaction diagram
-
-
-
?
1,1,1-trifluoropropane + reduced acceptor + H+ + O2
(2R)-1,1,1-trifluoropropan-2-ol + (2S)-1,1,1-trifluoropropan-2-ol + acceptor + H2O
show the reaction diagram
-
-
the S stereoisomer is the dominant product
-
?
1-butene + reduced acceptor + H+ + O2
1,2-epoxybutane + acceptor + H2O
show the reaction diagram
-
-
-
-
?
2 1-butene + 2 reduced acceptor + 2 H+ + 2 O2
3-buten-2-ol + 1,2-epoxybutane + 2 acceptor + 2 H2O
show the reaction diagram
-
-
-
-
?
2 butane + 2 reduced acceptor + 2 H+ + 2 O2
1-butanol + 2-butanol + 2 acceptor + 2 H2O
show the reaction diagram
-
-
-
-
?
2 pentane + 2 reduced acceptor + 2 H+ + 2 O2
1-pentanol + 2-pentanol + 2 acceptor + 2 H2O
show the reaction diagram
-
-
-
-
?
2 propane + 2 reduced acceptor + 2 H+ + 2 O2
1-propanol + 2-propanol + 2 acceptor + 2 H2O
show the reaction diagram
-
-
-
-
?
3 cis-2-butene + reduced acceptor + H+ + O2
meso-2,3-dimethyloxirane + acceptor + H2O
show the reaction diagram
-
-
-
-
?
3,3,3-trifluoroprop-1-ene + reduced acceptor + H+ + O2
(2S)-2-(trifluoromethyl)oxirane + (2R)-2-(trifluoromethyl)oxirane + acceptor + H2O
show the reaction diagram
-
-
the S stereoisomer is the dominant product
-
?
3,3,3-trifluoropropene + reduced acceptor + H+ + O2
3,3,3-trifluoro-1,2-epoxypropane + acceptor + H2O
show the reaction diagram
-
-
-
-
?
cis-but-2-ene + reduced acceptor + H+ + O2
cis-2,3-dimethyloxirane + acceptor + H2O
show the reaction diagram
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
show the reaction diagram
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
show the reaction diagram
methane + succinate + O2
methanol + fumarate + H2O
show the reaction diagram
membrane-bound enzyme only
-
-
?
Mn2+ + H2O2
?
show the reaction diagram
n-butane + reduced acceptor + O2
2-butanol + acceptor + H2O
show the reaction diagram
-
-
-
?
n-pentane + reduced acceptor + O2
2-pentanol + acceptor + H2O
show the reaction diagram
-
-
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
show the reaction diagram
propylene + 2,3-dimethylquinol + O2
propylene oxide + 2,3-dimethylquinone + H2O
show the reaction diagram
-
-
-
-
?
propylene + coenzyme Q0 + O2
propylene oxide + reduced coenzyme Q0 + H2O
show the reaction diagram
-
-
-
-
?
propylene + decyl-plastoquinol + O2
propylene oxide + decyl-plastoquinone + H2O
show the reaction diagram
-
higher activity compared to duroquinol
-
-
?
propylene + decylubiquinol + O2
propylene oxide + decylubiquinone + H2O
show the reaction diagram
-
-
-
-
?
propylene + duroquinol + O2
propylene epoxide + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
show the reaction diagram
-
-
-
-
?
propylene + menaquinol + O2
propylene oxide + menaquinone + H2O
show the reaction diagram
-
-
-
-
?
propylene + trimethylquinol + O2
propylene oxide + trimethylquinone + H2O
show the reaction diagram
-
-
-
-
?
trans-2-butene + reduced acceptor + H+ + O2
2,3-dimethyloxirane + acceptor + H2O
show the reaction diagram
-
-
-
-
?
trans-but-2-ene + reduced acceptor + H+ + O2
(2R,3R)-trans-2,3-dimethyloxirane + (2S,3S)-trans-2,3-dimethyloxirane + acceptor + H2O
show the reaction diagram
-
-
the S,S stereoisomer is the dominant product
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
show the reaction diagram
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
show the reaction diagram
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
duroquinol
NADH passes electron to duroquinol
NADPH
quinol
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
the enzyme contains three Co2+ ions per enzyme molecule
copper
Fe
-
pMMOH bears a binuclear iron valence site [Fe(III)-Fe(IV)]
Mn2+
-
pMMO, low content
Mo2+
-
pMMO, low content
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
copper
copper contents per 100 kDa alphabetagamma protomer of 15-20, eight to ten, two to three and two. Mixture of Cu(I) and Cu(II), copper cluster with a short Cu-Cu distance of 2.51 A that increases to 2.65 A upon chemical reduction with dithionite. The pMMO contains a mononuclear type 2Cu(II) centre and some type of copper cluster
Fe2+
0.75 to two iron ions per protomer. Di-iron may be the pMMO active site
Zinc
site within the membrane that can be occupied by zinc or copper
2-Heptyl-4-hydroxyquinoline-N-oxide
-
pMMO, at 0.05 mM
Acetylene
copper
-
two-coordinate (His2) mononuclear copper site and an anomalous site modeled as a dinuclear copper cluster. The cluster has one Cu ion bound by two His imidazoles and another by an imidazole and amino group of the pmoB N-terminal His
cyanide
-
less than 2% residual activity at 2 mM
duroquinol
-
increasing duroquinol concentration above 70 mM causes almost total inhibition of enzyme activity
duroquinone
-
noncompetitive inhibitor
EDTA
-
18.1% residual activity at 1.5 mM
Fe2+
-
slightly, membrane-bound enzyme form
Myxothiazol
-
pMMO, suicide substrate
NaCl
-
decrease in activity might be due to reduced enzyme solubility with increasing NaCl concentrations
propylene oxide
-
product inhibition at higher concentration
Zinc
-
a zinc site, probably adventitious, as the crystallization medium requires the metal. Purified pMMO does not contain zinc in the trans-membrane domain
Zn2+
effects of zinc binding on pMMO in membrane extracts, binding efficiency varies under different consitions, multisite inhibition, detailed overview. Addition of copper to these zinc-loaded membranes results in loss of half the zinc ions
additional information
inhibitor docking study, computational simulation of the structure and mechanism, modeling, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bacteriohemerythrin
-
enhances enzyme activity. The maximum activity is observed at a enzyme to bacteriohemerythrin concentration ratio of 4:1
-
Cu2+
-
pMMO, optimal at 0.3 mM
Fe3+
-
pMMO, optimal at 5.0 mM
lauryl maltoside
-
the stimulatory effect of lauryl maltoside is responsible for the initial increase in duroquinol-dependent activity of the pellet, but no activity with NADH is observed after this solubilization
methanobactin-Cu2+ complex
-
stimulation by methanobactin-Cu2+ complex, no activation in absence of copper, methanobactin is isolated from Methylosinus trichosporium strain OB3b
-
NDH-2
type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview
-
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
inhibition kinetic study
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.011
-
purified enzyme form pMMO
0.016
using propylene as substrate, pH and temperature not specified in the publication
0.034
-
purified enzyme, substrates propylene and duroquinol
0.0605
-
whole cells, substrate formate
0.1037
-
at 45°C and pH 7.0, with NADH as cosubstrate, in the presence of bacteriohemerythrin
0.114
-
membrane-bound enzyme, substrates propylene and duroquinol
0.1228
-
at 45°C and pH 7.0, with duroquinol as cosubstrate, in the presence of bacteriohemerythrin
0.16
-
purified enzyme
0.23
-
membrane-bound enzyme, substrates propylene and NADH
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.3
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
two distinct enzyme forms exist: a soluble cytoplasmic sMMO and a membrane-bound particulate pMMO
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
inactivation of the particulate methane monooxygenase (pMMO): the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit. LC-MS/MS analysis of the peptides derived from in-gel proteolytic digestion of the protein subunit identifies K196 of PmoC as the site of acetylation. No evidence is obtained for chemical modification of the PmoA or PmoB subunit. The inactivation of pMMO by a single adduct in the transmembrane PmoC domain is intriguing given the complexity of the structural fold of this large membrane-protein complex as well as the complicated roles played by the various metal cofactors in the enzyme catalysis. Computational studies suggest that the entry of hydrophobic substrates to, and migration of products from, the catalytic site of pMMO are controlled tightly within the transmembrane domain
metabolism
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
200000
-
non-denaturing PAGE
22000
-
1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
220000
-
purified pMMO-detergent complex, gel filtration
23000
24000
-
1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
25000
26000
27000
28328
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
390000
-
gel filtration
42785
42786
-
1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
45000
47000
660000
-
solubilized enzyme, gel filtration
99000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
hexamer
-
alpha2beta2gamma2
oligomer
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
trimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.8 A resolution
enzyme pMMO crystal structure analysis, PDB ID 3RGB
heterotrimer of three subunits, pmoA, pmoB, and pmoC, with a solvent-exposed domain above the trans-membrane domain, which consists of alpha-helices
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H137A/H139A
-
the mutant of subunit domain spmoB disrupts the dicopper site and exhibits no activity
H33A/H137A/H137A/H139A/H48N
site-directed mutagenesis
H33A/H137A/H139A
site-directed mutagenesis
H48N/H137A/H139A
-
the mutant of subunit domain spmoB disrupts the dicopper site and exhibits no activity
H72A
site-directed mutagenesis
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
or below: pMMO is irreversibly inactivated
438952
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pMMO is very unstable in vitro
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to O2, 3 kinetically distinct froms of pMMO with respect to O2 tension, type I is stable with moderate activity, type II is highly unstable to oxygen, type III is an intermediate form
-
438952
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, pMMO is stable to proteolysis for many months
-
-80°C, pMMO kinetically type I with respect to O2-sensitivity, repeated freeze-thaw-cycles, stable
-
4°C, pMMO is stable to proteolysis for 1-2 weeks
-
4°C, reducing argon or nitrogen atmosphere, no loss of activity after 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose Fast Flow column chromatography, lysine agarose column chromatography, Sephacryl S-300HR gel filtration, QEA-Sephadex A-50 column chromatography, and Sephacryl S200 gel filtration, Superdex 200 gel filtration, or ammonium sulfate precipitation followed by Source 30Q column chroamtography
-
FPLC liquid chromatography and Mono Q HR 5/50 GL column chromatography
-
membrane-associated methane-oxidizing complex consisting of the particulate methane mono-oxygenase, pMMOH, and an unidentified component, assigned as a potential particulate methane mono-oxygenase reductase, pMMOR
-
MonoQ 10/100 GL column chromatography and Sephacryl S100 gel filtration
-
native holoenzyme from isolated membranes by solubilization with detergent n-dodecyl beta-D-maltoside, ultrafiltration, and gel filtration
Ni2+-Sepharose Fast Flow column chromatography
-
optimization of solubilization and purification procedure for the hydroxylase component of membrane-bound enzyme, purification to homogeneity involves solubilization by dodexylbeta-D-maltoside, ion exchange chromatography and gel filtration, the purification includes the loss of the reductase component
-
partially by preparation of washed membranes
-
particulate form of methane hydroxylase (pMH) obtained by ion exchange and hydrophobic chromatography
-
pMMO after induction with copper, kinetic type I with respect to O2-sensitivity
-
stable and active native pMMO from membranes, by solubilization with 1% w/v CHAPS, removal of soluble proteins, gel filtration, anion exchange chromatography, and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) or Rosetta (DE3) pLysS cells
-
genetic analysis of pMMO genes
-
recombinant expression of wild-type holoenzyme and truncated recombinant periplasmic domains of pMMO (spmoB)
two aqueous-exposed subdomains toward the N- and C-termini of the large subunit are expressed in Escherichia coli BL21 (DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
pMMO is expressed at high copper/biomass ratios
-
pMMO is produced when the copper/biomass ratio is high
-
the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
energy production
teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Zahn, J.A.; DiSpirito, A.A.
Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
J. Bacteriol.
178
1018-1029
1996
Methylococcus capsulatus, Methylococcus capsulatus Bath
Manually annotated by BRENDA team
Nguyen, H.H.T.; Elliott, S.J.; Yip, J.H.K.; Chan, S.I.
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
Manually annotated by BRENDA team
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
417-427
2003
Methylococcus capsulatus, Methylococcus capsulatus Bath
Manually annotated by BRENDA team
Choi, D.W.; Kunz, R.C.; Boyd, E.S.; Semrau, J.D.; Antholine, W.E.; Han, J.I.; Zahn, J.A.; Boyd, J.M.; de la Mora, A.M.; DiSpirito, A.A.
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lieberman, R.L.; Kondapalli, K.C.; Shrestha, D.B.; Hakemian, A.S.; Smith, S.M.; Telser, J.; Kuzelka, J.; Gupta, R.; Borovik, A.S.; Lippard, S.J.; Hoffman, B.M.; Rosenzweig, A.C.; Stemmler, T.L.
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Anthony, C.
A tribute to Howard Dalton and methane monooxygenase
Sci. Prog.
91
401-415
2008
Methylococcus capsulatus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team