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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.18.3 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)

EC Number Crystallization (Comment) Organism
1.14.13.25 enzyme sMMO crystal structure analysis, PDB ID 1MTY Methylococcus capsulatus
1.14.18.3 enzyme pMMO crystal structure analysis, PDB ID 3RGB Methylococcus capsulatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.25 cytoplasm
-
 Methylococcus capsulatus 5737
-
1.14.13.25 soluble
-
 Methylococcus capsulatus
-
-
1.14.18.3 membrane membrane-bound Methylococcus capsulatus 16020
-
1.14.18.3 membrane membrane-bound Methylocystis sp. M 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.25 Fe2+ enzyme sMMO contains a non-heme diiron active site Methylococcus capsulatus
1.14.13.25 Iron the diiron active site of each homodimer is located in the alpha subunit, and no other metal centers are present. The resting state active site (MMOHox) consists of two Fe(III) ions coordinated by Glu114, His147, and a solvent molecule (Fe1), and Glu209, Glu243, and His246 (Fe2). The iron ions are 3.1 A apart, coordinated in pseudooctahedral fashion and bridged by two solvent molecules as well as Glu144 Methylococcus capsulatus
1.14.13.25 additional information the enzyme does not contain and require Cu2+ for activity Methylococcus capsulatus
1.14.18.3 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
1.14.18.3 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
1.14.18.3 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.
1.14.18.3 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
1.14.18.3 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
1.14.18.3 Zn2+ binds in the copper active site Methylococcus capsulatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.25 251000
-
-
 Methylococcus capsulatus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylococcus capsulatus
-
-
-
1.14.13.25 Methylococcus capsulatus P22869 and P18798 and P11987 and P18797 and P22868 and P22867 P22869 (MmoX), P18798 (MmoY), P11987 (MmoZ), P18797 (MmoB), P22868 (MmoC), P22867 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD)
-
1.14.13.25 Methylococcus capsulatus Bath
-
-
-
1.14.13.25 Methylococcus capsulatus Bath. P22869 and P18798 and P11987 and P18797 and P22868 and P22867 P22869 (MmoX), P18798 (MmoY), P11987 (MmoZ), P18797 (MmoB), P22868 (MmoC), P22867 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD)
-
1.14.18.3 Methylococcus capsulatus
-
-
-
1.14.18.3 Methylococcus capsulatus G1UBD1 AND Q607G3 alpha- and beta-subunits
-
1.14.18.3 Methylococcus capsulatus Bath G1UBD1 AND Q607G3 alpha- and beta-subunits
-
1.14.18.3 Methylococcus capsulatus Bath.
-
-
-
1.14.18.3 Methylocystis sp.
-
-
-
1.14.18.3 Methylocystis sp. M
-
-
-
1.14.18.3 Methylocystis sp. Rockwell
-
-
-
1.14.18.3 Methylosinus trichosporium
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.25 methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O reaction mechanism and reaction cycle of enzyme sMMO, via O2 activation intermediates, detailed overview Methylococcus capsulatus
a
1.14.18.3 methane + quinol + O2 = methanol + quinone + H2O reaction mechanism of enzyme pMMO, via O2 activation intermediates, detailed overview Methylococcus capsulatus
a
1.14.18.3 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + NAD(P)H + H+ + O2
-
 Methylococcus capsulatus methanol + NAD(P)+ + H2O
-
 ?
1.14.13.25 methane + NAD(P)H + H+ + O2
-
 Methylococcus capsulatus Bath. methanol + NAD(P)+ + H2O
-
 ?
1.14.13.25 methane + NADH + H+ + O2
-
 Methylococcus capsulatus methanol + NAD+ + H2O
-
 ?
1.14.13.25 methane + NADH + H+ + O2
-
 Methylococcus capsulatus Bath methanol + NAD+ + H2O
-
 ?
1.14.13.25 methane + NADH + H+ + O2
-
 Methylococcus capsulatus Bath. methanol + NAD+ + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylococcus capsulatus methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylocystis sp. M methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylococcus capsulatus Bath methanol + quinone + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2
-
 Methylococcus capsulatus methanol + acceptor + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2
-
 Methylococcus capsulatus Bath methanol + acceptor + H2O
-
 ?
1.14.18.3 methane + succinate + O2 membrane-bound enzyme only Methylococcus capsulatus methanol + fumarate + H2O
-
 ?
1.14.18.3 methane + succinate + O2 membrane-bound enzyme only Methylococcus capsulatus Bath methanol + fumarate + H2O
-
 ?
1.14.18.3 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 ?
-
 ?
1.14.18.3 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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.25 More enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview Methylococcus capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.14.13.25 sMMO
-
 Methylococcus capsulatus
1.14.13.25 soluble methane monooxygenase
-
 Methylococcus capsulatus
1.14.18.3 pMMO
-
 Methylococcus capsulatus
1.14.18.3 pMMO
-
 Methylosinus trichosporium
1.14.18.3 pMMO
-
 Methylocystis sp.
1.14.18.3 pMMO
-
 Methylocystis sp. M

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 NADH
-
 Methylococcus capsulatus
1.14.18.3 quinol
-
 Methylococcus capsulatus
1.14.18.3 quinol
-
 Methylocystis sp. M

General Information

EC Number General Information Comment Organism
1.14.13.25 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. Enzyme sMMO belongs to the larger bacterial multicomponent monooxygenase (BMM) family. 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
1.14.13.25 additional information enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview Methylococcus capsulatus
1.14.18.3 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
1.14.18.3 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
1.14.18.3 additional information enzyme pMMO contains a copper active site, active site structure, overview Methylocystis sp. M
1.14.18.3 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
1.14.18.3 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
1.14.18.3 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