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Literature summary for 1.14.13.25 extracted from

  • Mitic, N.; Schwartz, J.K.; Brazeau, B.J.; Lipscomb, J.D.; Solomon, E.I.
    CD and MCD studies of the effects of component B variant binding on the biferrous active site of methane monooxygenase (2008), Biochemistry, 47, 8386-8397.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
T111Y the T111Y variant of MMOB causes only a small increase in reactivity Methylosinus trichosporium

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ contains Fe2+ Methylosinus trichosporium

Organism

Organism UniProt Comment Textmining
Methylosinus trichosporium
-
-
-

Reaction

Reaction Comment Organism Reaction ID
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O catalyzes the oxidation of methane through the activation of O2 at a nonheme biferrous center in the hydroxylase component MMOH Methylosinus trichosporium
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + NAD(P)H + H+ + O2
-
 Methylosinus trichosporium methanol + NAD(P)+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
MMOB cofactor-free, monomeric component of sMMO, has regulatory role in catalysis Methylosinus trichosporium
MMOH hydroxylase component of sMMO, contains a binuclear nonheme iron active site that is essential for O2 activation and subsequent methane oxidation Methylosinus trichosporium
MMOR reductase component of sMMO, contains a FAD cofactor and a [2Fe-2S] cluster, is responsible for transferring the reducing equivalents from NAD(P)H to MMOH Methylosinus trichosporium
sMMO
-
 Methylosinus trichosporium

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Methylosinus trichosporium
NADH
-
 Methylosinus trichosporium
NADPH
-
 Methylosinus trichosporium