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Literature summary for 1.14.13.25 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

Inhibitors Comment Organism Structure
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
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]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Methylococcus capsulatus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methane + NADH + O2 Methylococcus capsulatus
-
methanol + NAD+ + H2O
-
?
methane + NADH + O2 Methylococcus capsulatus Bath
-
methanol + NAD+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
-
-
Methylococcus capsulatus Bath
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + NADH + O2
-
Methylococcus capsulatus methanol + NAD+ + H2O
-
?
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
-
?
methane + NADH + O2
-
Methylococcus capsulatus Bath methanol + NAD+ + H2O
-
?
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

Subunits Comment Organism
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

Synonyms Comment Organism
sMMO
-
Methylococcus capsulatus
soluble methane monooxygenase
-
Methylococcus capsulatus

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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