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Literature summary extracted from

  • Blazyk, J.L.; Gassner, G.T.; Lippard, S.J.
    Intermolecular electron-transfer reactions in soluble methane monooxygenase: a role for hysteresis in protein function (2005), J. Am. Chem. Soc., 127, 17364-17376.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.25 protein MMOB inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview Methylococcus capsulatus
1.14.13.25 protein MMOD inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview Methylococcus capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.25 additional information
-
additional information thermodynamics, stopped-flow kinetics, time-course profiles for MMOH reduction by MMOR ferredoxin and by MMOR3e- Methylococcus capsulatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.25 soluble
-
Methylococcus capsulatus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.25 Fe2+ the [2Fe-2S] cofactor of MMOR is a one-electron carrier, the ferredoxin center must transfer two electrons sequentially to MMOH to reduce fully each diiron(III) hydroxylase active site, overview 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 + O2 Methylococcus capsulatus
-
methanol + NAD+ + H2O
-
?
1.14.13.25 methane + NADH + O2 Methylococcus capsulatus Bath
-
methanol + NAD+ + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylococcus capsulatus
-
-
-
1.14.13.25 Methylococcus capsulatus Bath
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.25 methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O distribution of electrons in intermolecular electron-transfer intermediates, isomerization of the initial ternary complex is required for maximal electron-transfer rates Methylococcus capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + NADH + O2
-
Methylococcus capsulatus methanol + NAD+ + H2O
-
?
1.14.13.25 methane + NADH + O2 modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview Methylococcus capsulatus methanol + NAD+ + H2O
-
?
1.14.13.25 methane + NADH + O2
-
Methylococcus capsulatus Bath methanol + NAD+ + H2O
-
?
1.14.13.25 methane + NADH + O2 modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview Methylococcus capsulatus Bath methanol + NAD+ + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.14.13.25 More enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, 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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.25 4
-
assay at Methylococcus capsulatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.25 7
-
assay at Methylococcus capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 FAD
-
Methylococcus capsulatus
1.14.13.25 Ferredoxin several MMOR ferredoxin analogues, intermolecular electron transfer from ferredoxin analogues to hydroxylase protein MMOH, redox potential determinations, overview Methylococcus capsulatus
1.14.13.25 NADH
-
Methylococcus capsulatus