1.14.18.3: methane monooxygenase (particulate)
This is an abbreviated version!
For detailed information about methane monooxygenase (particulate), go to the full flat file.
Word Map on EC 1.14.18.3
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1.14.18.3
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pmmos
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methanotrophs
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methylococcus
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capsulatus
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bath
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methylocystis
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methylosinus
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ch4
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trichosporium
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pmocab
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methylomicrobium
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duroquinol
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environmental protection
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analysis
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trinuclear
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nadh:quinone
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monocopper
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diiron
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ammonia-oxidizing
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energy production
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degradation
- 1.14.18.3
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pmmos
- methanotrophs
- methylococcus
- capsulatus
- bath
- methylocystis
- methylosinus
- ch4
- trichosporium
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pmocab
- methylomicrobium
- duroquinol
- environmental protection
- analysis
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trinuclear
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nadh:quinone
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monocopper
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diiron
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ammonia-oxidizing
- energy production
- degradation
Reaction
Synonyms
copper-containing membrane monooxygenase, copper-containing membrane-bound monooxygenase, CuMMO, membrane-associated methane monooxygenase, membrane-bound methane monooxygenase, membrane-embedded methane monooxygenase, methane hydroxylase, mMMO, MMO, particulate methane mono-oxygenase, particulate methane monooxygenas, particulate methane monooxygenase, particulate methane monooxygenase A, particulate methane-oxidizing complex, particulate MMO, PMH, pMMO, pMMO hydroxylase, pMMO-H, pMMO1, pMMO2, PmoA, PmoB, sMMO, soluble methane monooxygenase, spmoB
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Metals Ions
Metals Ions on EC 1.14.18.3 - methane monooxygenase (particulate)
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copper
Cu+
Cu2+
Fe2+
Fe3+
Iron
Zinc
Zn2+
additional information
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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
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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
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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
the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron
copper
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the enzyme contains about 2.3 copper ions per 100 kDa protomer the enzyme contains a mixture of Cu+ and Cu2+
copper
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the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron
copper
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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
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the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron
copper
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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
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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
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pMMO, requirement for, contains 12-15 Cu+ ions per molecule of enzyme
Cu+
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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+
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14.5 atoms per molecule of enzyme pMMO, type II copper centre
Cu2+
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stimulation by methanobactin-Cu2+ complex, no activation in absence of methanobactin
Cu2+
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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+
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contains a mononuclear and a dinculear Cu2+ center in the soluble domain of the 47 kDa subunit
Cu2+
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multicopper enzyme, contains 3 Cu2+ ions per trimer, contains 13.6 copper atoms per protein complex
Cu2+
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pMH contains 2-4 atoms of copper per a minimum molecular weight of 99 kDa
Cu2+
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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+
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pMMO contains a dicopper center and a mononuclear copper center, As-isolated enzyme conatins 10.2 Cu2+ equivalents per 100 kDa pMMO
Cu2+
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the active enzyme contains approximately 15 copper atoms per mol
Cu2+
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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+
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+
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a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity
Cu2+
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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+
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the active enzyme contains approximately 15 copper atoms per mol enzyme
Cu2+
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copper genetically regulates the enzyme activity of the soluble and membrane-bound form
Cu2+
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increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1
Cu2+
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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+
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a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity
Fe2+
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As-isolated enzyme conatins 1.31 Fe2+ equivalents per 100 kDa pMMO
Fe2+
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pmMO contains 450 nmol Fe2+ per mg protein in membrane fractions
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presence of an octahedral environment that may well be exchange-coupled to another paramagnetic species
Iron
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the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme, contains EPR-silent iron
Zn2+
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the enzyme contains a nonphysiological mononuclear zinc center
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+
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increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1
Zn2+
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pmMO contains 1.5 nmol Zn2+ per mg protein in membrane fractions
additional information
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analysis of the oxidation states and coordination environments of the pMMO metal centers, overview
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
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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
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increase of activity is not observed by adding FeSO4
additional information
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purified pMMO contains no iron per pMMO protomer
additional information
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purified pMMO does not contain zinc in the trans-membrane domain