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
ECTree
1.14.18.3 methane monooxygenase (particulate)Advanced search results
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results (Inhibitors
Inhibitors on EC 1.14.18.3 - methane monooxygenase (particulate)
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
duroquinol
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increasing duroquinol concentration above 70 mM causes almost total inhibition of enzyme activity
H2O2
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reversible inhibition of pMMO with H2O2 upon treatment of pMMO with H2O2 followed by the addition of catalase. H2O2 re-oxidizes the type 2 copper in pMMO reduced with duroquinol
NaCl
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decrease in activity might be due to reduced enzyme solubility with increasing NaCl concentrations
Acetylene
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is a competitive inhibitor of pMH, interacts with its substrate-binding center
Acetylene
a suicide inhibitor of pMMO, 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 fromin-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
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
copper
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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
copper
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contains approximately two copper ions per 100 kDa protomer, type 2 Cu(II) present as two distinct species, mixture of Cu(I) and Cu(II). Short Cu-Cu interaction at 2.51 A. Di-copper centre plays an important functional role in pMMO, whereas the mononuclear copper centre is not critical
cyanide
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cyanide treatment of the enzyme removes about 98% of the copper and about 49% of the iron and abolishes all activity
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
Zinc
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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
Zn2+
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zinc inhibits enzyme pMMO at two sites that are distinct from the copper active site, zinc might inhibit proton transfer in pMMO. Locations for the two zinc inhibition sites: the first is the crystallographic zinc site in the pmoC subunit, a second zinc site is present on the cytoplasmic side of the pmoC subunit
additional information
inhibitor docking study, computational simulation of the structure and mechanism, modeling, overview
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