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Literature summary for 1.14.13.25 extracted from

  • Zhang, J.; Zheng, H.; Groce, S.L.; Lipscomb, J.D.
    Basis for specificity in methane monooxygenase and related non-heme iron-containing biological oxidation catalysts (2006), J. Mol. Catal. A, 251, 54-65.
No PubMed abstract available

Application

Application Comment Organism
synthesis the enzyme is a base or scaffold for design of small molecule catalysts for use in large scale methanol synthesis Methylophilaceae

Protein Variants

Protein Variants Comment Organism
additional information mutagenesis of MMOB potentially broadening the substrate range of the enzyme Methylophilaceae

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme contains a Fe2S2 cluster, a bis-my-hydroxo-bridged dinuclear iron cluster, that binds to the enzyme reductase domain MMOR Methylophilaceae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methane + NADH + O2 Methylophilaceae methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2 methanol + NAD+ + H2O
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additional information Methylophilaceae access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview ?
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Organism

Organism UniProt Comment Textmining
Methylophilaceae
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Reaction

Reaction Comment Organism Reaction ID
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O reaction mechanism and regulation, catalytic cycle of sMMO, the enzyme complex causes quantum tunneling to dominate in CĀ–H bond cleavage reaction for methane, selectively increasing the rate for this substrate, mechanism of C-H bond cleavage, overview Methylophilaceae

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:methane-grown cell
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Methylophilaceae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + NADH + O2 methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2 Methylophilaceae methanol + NAD+ + H2O
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methane + NADH + O2 for the MMOH alone the rate of turnover is increased 150fold and rate constant for O2 binding is increased 1000fold in the binary complex compared to the complete enzyme Methylophilaceae methanol + NAD+ + H2O
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additional information access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview Methylophilaceae ?
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?

Subunits

Subunits Comment Organism
More three-dimensional structure, the enzyme consists as three protein component system, the regulatory protein MMOB, containing Fe2S2 cluster and a FAD cofactor, binds to the active site-containing hydroxylase protein creating a pore sized for methane into the active site, the third component is termed B, the complex appears to cause quantum tunneling to dominate in CĀ–H bond cleavage reaction for methane, selectively increasing the rate for this substrate, overview Methylophilaceae

Synonyms

Synonyms Comment Organism
sMMO
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Methylophilaceae
soluble methane monooxygenase
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Methylophilaceae

Cofactor

Cofactor Comment Organism Structure
FAD binds to the enzyme reductase protein MMOR Methylophilaceae
NADH binds to the enzyme hydroxylase protein MMOH Methylophilaceae