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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
-
?
1,3-butadiene + duroquinol + O2
1,2-epoxybut-3-ene + duroquinone + H2O
-
-
100% 1,2-epoxybut-3-ene is produced, 36% (R)-selectivity, 64% (S)-selectivity
-
?
1-bromopropane + duroquinol + O2
1-bromo-2-propanol + 1-propanol + 1-bromo-3-propanol + duroquinone + H2O
-
-
72% 1-bromo-2-propanol (70% (R)-selectivity, 30% (S)-selectivity), 24% 1-propanol and 4% 1-bromo-3-propanol are produced
-
?
1-bromopropene + duroquinol + O2
1-bromo-2,3-epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
-
-
63% 1-bromo-2,3-epoxypropane, 31% allyl-alcohol and 6% 1-propanol are produced
-
?
1-butene + duroquinol + O2
1,2-epoxybutane + duroquinone + H2O
-
-
100% epoxybutane is produced, 36% (R)-selectivity, 64% (S)-selectivity
-
?
1-butene + reduced acceptor + H+ + O2
1,2-epoxybutane + acceptor + H2O
-
-
-
-
?
1-chloropropane + duroquinol + O2
1-chloro-2-propanol + 1-propanol + 1-chloro-3-propanol + duroquinone + H2O
-
-
64% 1-chloro-2-propanol (70% (R)-selectivity, 30% (S)-selectivity), 29% 1-propanol and 7% 1-chloro-3-propanol are produced
-
?
1-chloropropene + duroquinol + O2
1-chloro-2,3-epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
-
-
67% 1-chloro-2,3-epoxypropane, 23% allyl-alcohol and 10% 1-propanol are produced
-
?
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
-
-
-
-
?
2-bromopropane + duroquinol + O2
2-bromo-1-propanol + acetone + duroquinone + H2O
-
-
2-bromo-1-propanol shows 26% (R)-selectivity and 74% (S)-selectivity
-
?
2-chloropropane + duroquinol + O2
2-chloro-1-propanol + ? + duroquinone + H2O
-
-
1-chloro-2-propanol shows 26% (R)-selectivity and 74% (S)-selectivity
-
?
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
-
-
-
-
?
butane + duroquinol + O2
2-butanol + butanal + duroquinone + H2O
-
-
91% 2-butanal and 9% butanal are produced
-
?
cis-2-butene + duroquinol + O2
cis-2,3-epoxybutane + duroquinone + H2O
-
-
cis-2,3-epoxybutane is produced
-
?
cis-but-2-ene + reduced acceptor + H+ + O2
cis-2,3-dimethyloxirane + acceptor + H2O
-
-
-
-
?
ethane + duroquinol + O2
ethanal + duroquinone + H2O
-
-
100% ethanal is produced
-
?
ethylene + duroquinol + O2
epoxyethane + duroquinone + H2O
-
-
100% epoxyethane produced
-
?
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
methane + trans-dichloroethylene + vinyl chloride + trichloroethylene + O2
?
-
-
-
-
?
n-butane + reduced acceptor + O2
2-butanol + acceptor + H2O
n-pentane + reduced acceptor + O2
2-pentanol + acceptor + H2O
pentane + duroquinol + O2
2-pentanol + pentanal + duroquinone + H2O
-
-
31% 2-pentanal and 69% pentanal are produced
-
?
propane + duroquinol + O2
2-propanol + propanal + duroquinone + H2O
-
-
84% 2-propanal and 16% propanal are produced
-
?
propene + duroquinol + O2
1,2-epoxypropane + duroquinone + H2O
-
-
57% (R)-selectivity, 43% (S)-selectivity
-
?
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
propylene + decylubiquinol + O2
propylene oxide + decylubiquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
-
-
95% epoxypropane, 4.6% allyl-alcohol and 0.4% butanal are produced
-
?
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 + duroquinol + O2
trans-2,3-epoxybutane + trans-2-butane-1-al + duroquinone + H2O
-
-
41% trans-2,3-epoxybutane and 59% trans-2-butane-1-al are produced
-
?
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 + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
100% methanol is produced
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + O2
methanol + NAD+ + 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 + 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
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
enzyme pMMO activity is dependent on oxygen concentrations
-
-
?
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
-
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
methane activation occurs at the Cu centers of particulate methane monooxygenase
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
-
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
methane activation occurs at the Cu centers of particulate methane monooxygenase
-
-
?
methane + quinol + O2
methanol + quinone + H2O
-
methane activation occurs at the Cu centers of particulate methane monooxygenase
-
-
?
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
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
in the presence of pMMO substrate methane, the H2O2 formation is diminished, which is likely to be caused by the consumption of electrons by methane oxidation
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
Q25BV2; Q25BV3; Q25BV4, Q25BV9; Q25BW0; Q25BW2; Q25BW3
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
Q25BV2; Q25BV3; Q25BV4, Q25BV9; Q25BW0; Q25BW2; Q25BW3
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
Soil bacterium
-
pmoA cluster JR3 may be the most important methane oxidizer for arid soils
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
D0FK34, D0FK37, D0FK39, D0FK43, D0FK44, D0FK45, D0FK53, D0FK57, D0FK58, D0FK59, D0FK61, D0FK62, D0FK63, D0FK65, D0FK67, D0FKJ4, D0FKK3, D0FKS0, D0FL26, D0FL48 -
-
-
?
methane + succinate + O2
methanol + fumarate + H2O
membrane-bound enzyme only
-
-
?
methane + succinate + O2
methanol + fumarate + H2O
membrane-bound enzyme only
-
-
?
Mn2+ + H2O2
?
-
-
-
-
?
n-butane + reduced acceptor + O2
2-butanol + acceptor + H2O
-
-
-
?
n-butane + reduced acceptor + O2
2-butanol + acceptor + H2O
-
-
-
-
?
n-butane + reduced acceptor + O2
2-butanol + acceptor + H2O
-
-
-
-
?
n-pentane + reduced acceptor + O2
2-pentanol + acceptor + H2O
-
-
-
?
n-pentane + reduced acceptor + O2
2-pentanol + acceptor + H2O
-
-
-
-
?
n-pentane + reduced acceptor + O2
2-pentanol + acceptor + H2O
-
-
-
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
-
-
-
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
-
enzyme form sMMO
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
-
-
-
-
?
propene + reduced acceptor + H+ + O2
1,2-epoxypropane + acceptor + H2O
-
enzyme form sMMO
-
?
propylene + 2,3-dimethylquinol + O2
propylene oxide + 2,3-dimethylquinone + H2O
-
-
-
-
?
propylene + 2,3-dimethylquinol + O2
propylene oxide + 2,3-dimethylquinone + H2O
-
-
-
-
?
propylene + coenzyme Q0 + O2
propylene oxide + reduced coenzyme Q0 + 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 + decyl-plastoquinol + O2
propylene oxide + decyl-plastoquinone + H2O
-
higher activity compared to duroquinol
-
-
?
propylene + duroquinol + O2
propylene epoxide + duroquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene epoxide + duroquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
-
-
-
-
?
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
-
-
?
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
?
-
-
quinols are effective reductants for the detergent-solubilized enzyme, whereas NADH is ineffective
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
decyl-plastoquinol, reduced coenzyme Q1, and trimethylquinol can drive pMMO, though its activity is lower than that with duroquinol. Succinate-driven pMMO activity in the membrane fractions is also observed
-
-
?
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
?
-
-
duroquinol, an electron donor for pMMO may induce the formation of H2O2 by pMMO under aerobic conditions
-
-
?
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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
copper
-
contains 2.3 copper ions per 100 kDa protomer
copper
-
the enzyme contains about 2.3 copper ions per 100 kDa protomer the enzyme contains a mixture of Cu+ and Cu2+
copper
-
the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron
copper
-
the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase
copper
-
contains 4.8 copper ions per 100 kDa protomer
copper
-
the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron
copper
-
the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase
copper
-
an anomalous site modeled as a dinuclear copper cluster. The mononuclear copper site is absent (one His is not conserved), and the zinc replaced by a copper ion
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
Cu2+
-
the active enzyme contains approximately 15 copper atoms per mol
Cu2+
-
a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity
Cu2+
-
required for activity, enzyme pMMO has a copper active site. dicopper site occupied with a two copper ions or b one copper ion from Methylocystis speciesstrain M, structure comparisons, modeling
Cu2+
-
the active enzyme contains approximately 15 copper atoms per mol enzyme
Cu2+
-
required for activity
Cu2+
-
required for activity
Cu2+
-
pMMO contains tightly bound copper, EDTA has no effect
Cu2+
-
copper genetically regulates the enzyme activity of the soluble and membrane-bound form
Cu2+
-
increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1
Cu2+
-
pmMO contains copper ions (150 nmol per mg protein in membrane fractions) that are required for its enzymatic activity. Some increase in pMMO activity is observed by adding CuSO4
Cu2+
-
a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity
Cu2+
-
purified pMMO contains 2-3 coppers
Cu2+
the enzyme possesses a dicopper center
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
Fe2+
-
the active enzyme contains 2 iron atoms per mol
Fe2+
-
the enzyme contains about 0.6 Fe2+ ions per 100 kDa protomer
Fe2+
-
the active enzyme contains 2 iron atoms per mol enzyme
Fe2+
-
pmMO contains 450 nmol Fe2+ per mg protein in membrane fractions
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
Zinc
contains zinc
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
Zn2+
-
enzyme bound, structure analysis, overview
Zn2+
-
increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1
Zn2+
-
pmMO contains 1.5 nmol Zn2+ per mg protein in membrane fractions
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
additional information
-
the final model for the zinc-soaked structure included pmoB residues 29-418, pmoA residues 9-252, and pmoC residues 16-210 and 224-256, three polyalanine helices consisting of up to 25 residues, five zinc ions, three copper ions, and one cacodylate molecule
additional information
-
increase of activity is not observed by adding FeSO4
additional information
-
purified pMMO contains no iron per pMMO protomer
additional information
-
purified pMMO does not contain zinc in the trans-membrane domain
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evolution
methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available
evolution
-
methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available
evolution
-
the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily
evolution
-
the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily
evolution
the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily
evolution
-
methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available
-
evolution
-
the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily
-
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
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
-
ammonia-supplied Methylosinus trichosporium OB3b containing soluble methane monooxygenase (sMMO) grow at the fastest rate, while the highest poly-beta-hydroxybutyrate content is obtained by transferring nitrate-supplied bacteria with the expression of particulate methane monooxygenase (pMMO) to nitrogen-free mineral salts (NFMS) + 0.005 mmol/l Cu medium. The slightly lower growth rate and lower cell yield of ammonia supplied bacteria expressing particulate methane monooxygenase (pMMO) might be attributed to high similarity between the gene encoding particulate methane monooxygenase (pMMO) and the sequence of the ammoniamonooxygenase gene. The methane monooxygenase activity, growth rate and intracellular poly-beta-hydroxybutyrate content of bacteria expressing pMMO are greatly decreased after being continuously cultivated with N2. However, in the cyclic NO3-N2 cultivation regime, the activity of N2-fixing bacteria expressing pMMO is significantly increased
metabolism
during production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation
metabolism
in the initial steps of their metabolic pathway, methanotrophic bacteria oxidize methane to methanol with methane monooxygenases (MMOs) and methanol to formaldehyde with methanol dehydrogenases (MDHs). Membrane-bound particulate MMO (pMMO) and MDH interact to form a metabolic supercomplex, interaction analysis and biolayer interferometry studies demonstrate specific protein-protein interactions between methanol dehydrogenase (MDH) and Methyylococcus capsulatus (Bath) pMMO as well as between MDH and the truncated recombinant periplasmic domains of pMMO (spmoB), kinetics, overview
metabolism
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, analysis of the mechanism of the copper switch. Transcriptomic profiling of particulate MMO and soluble MMO, EC 1.14.13.25, using Methylococcus capsulatus DNA microarrays. 137 ORFs are found to be differentially expressed between cells producing sMMO and pMMO, while only minor differences in gene expression are observed between the pMMO-producing cultures. Of these, 87 genes are upregulated during sMMO-producing cells, i.e. during copper-limited growth. Major changes takes place in the respiratory chain between pMMO-and sMMO-producing cells, and quinone are predominantly used as the electron donors for methane oxidation by pMMO. Proposed pathway of methane oxidation in Methylococcus capsulatus cells producing either sMMO or pMMO, overview
metabolism
-
during production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation
-
metabolism
-
in the initial steps of their metabolic pathway, methanotrophic bacteria oxidize methane to methanol with methane monooxygenases (MMOs) and methanol to formaldehyde with methanol dehydrogenases (MDHs). Membrane-bound particulate MMO (pMMO) and MDH interact to form a metabolic supercomplex, interaction analysis and biolayer interferometry studies demonstrate specific protein-protein interactions between methanol dehydrogenase (MDH) and Methyylococcus capsulatus (Bath) pMMO as well as between MDH and the truncated recombinant periplasmic domains of pMMO (spmoB), kinetics, overview
-
metabolism
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, analysis of the mechanism of the copper switch. Transcriptomic profiling of particulate MMO and soluble MMO, EC 1.14.13.25, using Methylococcus capsulatus DNA microarrays. 137 ORFs are found to be differentially expressed between cells producing sMMO and pMMO, while only minor differences in gene expression are observed between the pMMO-producing cultures. Of these, 87 genes are upregulated during sMMO-producing cells, i.e. during copper-limited growth. Major changes takes place in the respiratory chain between pMMO-and sMMO-producing cells, and quinone are predominantly used as the electron donors for methane oxidation by pMMO. Proposed pathway of methane oxidation in Methylococcus capsulatus cells producing either sMMO or pMMO, overview
-
metabolism
-
during production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation
-
physiological function
methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO)
physiological function
-
methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO)
physiological function
MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol
physiological function
particulate methane monooxygenase (pMMO) can activate methane
physiological function
-
particulate methane monooxygenase (pMMO) can activate methane
-
physiological function
-
methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO)
-
physiological function
-
MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol
-
additional information
analysis of structural and functional differences of sMMO, EC 1.14.13.25, and pMMO, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview
additional information
-
enzyme pMMO contains a copper active site, active site structure, overview
additional information
-
enzyme pMMO contains a copper active site, active site structure, overview. Density functional theory and quantum mechanics/molecular mechanics calculations using the Methylococcus capsulatus pMMO structure as a starting model suggesting that a mononuclear copper active site may be viable, proceeding through a CuIII-oxo (CuII-O·) species
additional information
enzyme pMMO contains a copper active site, active site structure, overview. Density functional theory and quantum mechanics/molecular mechanics calculations using the Methylococcus capsulatus pMMO structure as a starting model suggesting that a mononuclear copper active site may be viable, proceeding through a CuIII-oxo (CuII-O·) species
additional information
-
nano-LC-ESI-MS/MS analysis for protein identification of purified Methylocystis sp. str. Rockwell pMMO. The final model for the zinc-soaked structure included pmoB residues 29-418, pmoA residues 9-252, and pmoC residues 16-210 and 224-256, three polyalanine helices consisting of up to 25 residues, five zinc ions, three copper ions, and one cacodylate molecule
additional information
-
structure-function relationship of copper-containing membrane monooxygenases
additional information
-
structure-function relationship of copper-containing membrane monooxygenases
additional information
structure-function relationship of copper-containing membrane monooxygenases
additional information
the enzyme has a dicopper active site, analysis of the resting state and a possible peroxo state of the dicopper active site of pMMO by using combined quantum mechanics and molecular mechanics calculations on the basis of reported X-ray crystal structure, PDB ID 1YEW, of the resting state of pMMO. 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. Possible Formation of a Peroxo Species in the Dicopper Site of pMMO, overview
additional information
-
the enzyme has a dicopper active site, analysis of the resting state and a possible peroxo state of the dicopper active site of pMMO by using combined quantum mechanics and molecular mechanics calculations on the basis of reported X-ray crystal structure, PDB ID 1YEW, of the resting state of pMMO. 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. Possible Formation of a Peroxo Species in the Dicopper Site of pMMO, overview
-
additional information
-
enzyme pMMO contains a copper active site, active site structure, overview. Density functional theory and quantum mechanics/molecular mechanics calculations using the Methylococcus capsulatus pMMO structure as a starting model suggesting that a mononuclear copper active site may be viable, proceeding through a CuIII-oxo (CuII-O·) species
-
additional information
-
structure-function relationship of copper-containing membrane monooxygenases
-
additional information
-
analysis of structural and functional differences of sMMO, EC 1.14.13.25, and pMMO, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview
-
additional information
-
nano-LC-ESI-MS/MS analysis for protein identification of purified Methylocystis sp. str. Rockwell pMMO. The final model for the zinc-soaked structure included pmoB residues 29-418, pmoA residues 9-252, and pmoC residues 16-210 and 224-256, three polyalanine helices consisting of up to 25 residues, five zinc ions, three copper ions, and one cacodylate molecule
-
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heterotrimer
-
heterotrimer
-
crystallography
heterotrimer
-
1 * 42785 + 1 * 29733 + 1 * 28328, MALDI-TOF mass spectrometry
heterotrimer
-
1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
heterotrimer
-
1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH
heterotrimer
-
pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
heterotrimer
-
1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry
heterotrimer
-
1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
heterotrimer
-
2 * 000, calculated from amino acid sequence
heterotrimer
alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits
heterotrimer
enzyme pMMO possesses an alpha3beta3gamma3 trimeric structure composed of the pmoB, pmoA, and pmoC polypeptides and multiple metal binding sites
heterotrimer
the enzyme consists of three subunits, pmoB, pmoA, and pmoC, organized in an alpha3beta3gamma3 trimer
heterotrimer
the pMMO is an about 300 kDa alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits. The pmoA and pmoC subunits are composed primarily of transmembrane helices, and pmoB consists of two periplasmic cupredoxin-like domains linked by two transmembrane helices. The active site is proposed to be a dinuclear copper center located in the N-terminal pmoB periplasmic domain close to the membrane interface
heterotrimer
three pMMO subunits confirmed by mass spectrometry
heterotrimer
-
1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry
-
heterotrimer
-
1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
-
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
-
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
-
heterotrimer
-
crystallography
-
heterotrimer
-
the pMMO is an about 300 kDa alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits. The pmoA and pmoC subunits are composed primarily of transmembrane helices, and pmoB consists of two periplasmic cupredoxin-like domains linked by two transmembrane helices. The active site is proposed to be a dinuclear copper center located in the N-terminal pmoB periplasmic domain close to the membrane interface
-
heterotrimer
-
the enzyme consists of three subunits, pmoB, pmoA, and pmoC, organized in an alpha3beta3gamma3 trimer
-
heterotrimer
-
alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits
-
heterotrimer
-
three pMMO subunits confirmed by mass spectrometry
-
heterotrimer
-
enzyme pMMO possesses an alpha3beta3gamma3 trimeric structure composed of the pmoB, pmoA, and pmoC polypeptides and multiple metal binding sites
-
heterotrimer
-
1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH
-
heterotrimer
-
pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
-
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
heterotrimer
-
three pMMO subunits confirmed by mass spectrometry
heterotrimer
-
three pMMO subunits confirmed by mass spectrometry
-
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
-
heterotrimer
-
1 * 40000 + 1 * 24000 + 1 * 21000, SDS-PAGE
hexamer
-
alpha2beta2gamma2
hexamer
-
alpha2beta2gamma2
-
oligomer
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
oligomer
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
-
trimer
-
1 * 45000 + 1 * 26000 + 1 * 23000, pMMO, SDS-PAGE
trimer
-
1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
trimer
-
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
trimer
1 * 26690, subunit pmoB + 1 * 29000, subunit pmoA, + 1 * 42000, subunit pmoB, SDS-PAGE
trimer
-
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
-
trimer
-
1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
-
trimer
-
1 * 45000 + 1 * 26000 + 1 * 23000, pMMO, SDS-PAGE
-
trimer
-
1 * 26690, subunit pmoB + 1 * 29000, subunit pmoA, + 1 * 42000, subunit pmoB, SDS-PAGE
-
additional information
-
pMMO subunit A has acetylene binding ability
additional information
enzyme structure comparisons, overview
additional information
enzyme pMMO is a large protein complex with three subunits, PmoA, PmoB and PmoC, and many copper ions, three-dimensional structure of pMMO, overview
additional information
-
pMMO subunit A has acetylene binding ability
-
additional information
-
enzyme pMMO is a large protein complex with three subunits, PmoA, PmoB and PmoC, and many copper ions, three-dimensional structure of pMMO, overview
-
additional information
-
enzyme structure comparisons, overview
-
additional information
-
three-dimensional structure determination and analysis
additional information
-
enzyme structure comparisons, overview
additional information
-
three-dimensional structure determination and analysis
-
additional information
-
enzyme structure comparisons, overview
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