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Literature summary for 1.14.13.25 extracted from

  • Astier, Y.; Balendra, S.; Hill, H.A.; Smith, T.J.; Dalton, H.
    Cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode (2003), Eur. J. Biochem., 270, 539-544.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
catalase reduction current is enhanced by the presence of catalase ot if the reaction is performed in a flow-cell, probably because O2 is reduced to H2O2, by the hydroxylase component of the enzyme MMOH at the electrode surface and the H2O2 then inactivates the enzyme unless removed by catalase or a continous flow solution Methylococcus capsulatus

Application

Application Comment Organism
synthesis cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode. The electrochemically driven enzyme shows the same catalytic activity and regulation by the protein component B (MMOB) as the natural NAD(P)H-driven reaction and may have the potential for development into economic NAD(P)H-independent oxygenation catalyst Methylococcus capsulatus

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode Methylococcus capsulatus ?
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?

Synonyms

Synonyms Comment Organism
MMO
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Methylococcus capsulatus

Cofactor

Cofactor Comment Organism Structure
additional information cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode Methylococcus capsulatus