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Literature summary for 1.15.1.2 extracted from

  • Molina-Heredia, F.P.; Houee-Levin, C.; Berthomieu, C.; Touati, D.; Tremey, E.; Favaudon, V.; Adam, V.; Niviere, V.
    Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide (2006), Proc. Natl. Acad. Sci. USA, 103, 14750-14755.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Iron investigation on reactivity of the SOR–ferrocyanide complex with O2 radical by pulse and gamma-ray radiolysis, infrared, and UV-visible spectroscopies. A one-electron redox chemistry is carried out by the ferrocyanide moiety of the complex, whereas the SOR iron site remains in the reduced state. The toxic H2O2 species is no longer the reaction product Desulfarculus baarsii

Organism

Organism UniProt Comment Textmining
Desulfarculus baarsii
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme has O2 radical detoxification activity, catalyzed by the SOR-ferrocyanide complex, which does not conduct to the production of the toxic H2O2 species Desulfarculus baarsii ?
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