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Literature summary extracted from

  • Siewert, I.; Limberg, C.
    Low-molecular-weight analogues of the soluble methane monooxygenase (sMMO): from the structural mimicking of resting states and intermediates to functional models (2009), Chemistry, 15, 10316-10328.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.25 Fe2+ activation of dioxygen occurs at a diiron centre within the hydroxylase subunit. The monooxygenation of a substrate by sMMO requires only two oxidation equivalents, and, consequently, after the oxygenation the two iron centres remain in the oxidation state +III Bacteria

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Bacteria
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + NAD(P)H + O2 consists of three subunits, the hydroxylase (MMOH), at which the oxidation of methane takes place, the reductase (MMOR) and a small regulating unit MMOB Bacteria methanol + NAD(P)+ + H2O
-
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Synonyms

EC Number Synonyms Comment Organism
1.14.13.25 sMMO
-
Bacteria
1.14.13.25 soluble methane monooxygenase
-
Bacteria

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 NADH two-electron reduction of MMOHox by NADH mediated by MMOR enables further oxidation cycles Bacteria
1.14.13.25 NADPH
-
Bacteria