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Literature summary for 1.14.18.3 extracted from

  • Ross, M.O.; Rosenzweig, A.C.
    A tale of two methane monooxygenases (2017), J. Biol. Inorg. Chem., 22, 307-319 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.18.3

Activating Compound

Activating Compound Comment Organism Structure
NDH-2 type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview Methylococcus capsulatus

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme pMMO crystal structure analysis, PDB ID 3RGB Methylococcus capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Methylococcus capsulatus 16020
-
membrane membrane-bound Methylocystis sp. M 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
copper the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron Methylococcus capsulatus
copper the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron Methylosinus trichosporium
copper the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron Methylocystis sp.
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 Methylocystis sp. M
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 Methylococcus capsulatus
Zn2+ binds in the copper active site Methylococcus capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methane + quinol + O2 Methylococcus capsulatus
-
 methanol + quinone + H2O
-
 ?
methane + quinol + O2 Methylocystis sp. M
-
 methanol + quinone + H2O
-
 ?
methane + quinol + O2 Methylococcus capsulatus Bath
-
 methanol + quinone + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
-
-
Methylococcus capsulatus G1UBD1 AND Q607G3 alpha- and beta-subunits
-
Methylococcus capsulatus Bath G1UBD1 AND Q607G3 alpha- and beta-subunits
-
Methylococcus capsulatus Bath.
-
-
-
Methylocystis sp.
-
-
-
Methylocystis sp. M
-
-
-
Methylocystis sp. Rockwell
-
-
-
Methylosinus trichosporium
-
-
-

Reaction

Reaction Comment Organism Reaction ID
methane + quinol + O2 = methanol + quinone + H2O reaction mechanism of enzyme pMMO, via O2 activation intermediates, detailed overview Methylococcus capsulatus
a
methane + quinol + O2 = methanol + quinone + H2O reaction mechanism of enzyme pMMO, via O2 activation intermediates, detailed overview Methylocystis sp. M
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + quinol + O2
-
 Methylococcus capsulatus methanol + quinone + H2O
-
 ?
methane + quinol + O2
-
 Methylocystis sp. M methanol + quinone + H2O
-
 ?
methane + quinol + O2
-
 Methylococcus capsulatus Bath methanol + quinone + H2O
-
 ?
methane + reduced acceptor + H* + O2
-
 Methylococcus capsulatus methanol + acceptor + H2O
-
 ?
methane + reduced acceptor + H* + O2
-
 Methylococcus capsulatus Bath methanol + acceptor + H2O
-
 ?
methane + succinate + O2 membrane-bound enzyme only Methylococcus capsulatus methanol + fumarate + H2O
-
 ?
methane + succinate + O2 membrane-bound enzyme only Methylococcus capsulatus Bath methanol + fumarate + H2O
-
 ?
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 Methylococcus capsulatus ?
-
 ?
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 Methylococcus capsulatus Bath ?
-
 ?

Synonyms

Synonyms Comment Organism
pMMO
-
 Methylococcus capsulatus
pMMO
-
 Methylosinus trichosporium
pMMO
-
 Methylocystis sp.
pMMO
-
 Methylocystis sp. M

Cofactor

Cofactor Comment Organism Structure
quinol
-
 Methylococcus capsulatus
quinol
-
 Methylocystis sp. M

General Information

General Information Comment Organism
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 Methylococcus capsulatus
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 Methylocystis sp. M
additional information enzyme pMMO contains a copper active site, active site structure, overview Methylocystis sp. M
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 Methylococcus capsulatus
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) Methylococcus capsulatus
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) Methylocystis sp. M