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Literature summary extracted from

  • Mathe, C.; Weill, C.O.; Mattioli, T.A.; Berthomieu, C.; Houee-Levin, C.; Tremey, E.; Niviere, V.
    Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii (2007), J. Biol. Chem., 282, 22207-22216.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 gene sor, complementation of the Escherichia coli QC2375 mutant strain Desulfarculus baarsii

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.2 E114A the mutant shows significantly modified pulse radiolysis kinetics for the protonation process of the first reaction intermediate compared to the wild-type enzyme, mutation results in both a strengthening of the S-Fe bond and an increase in the extent of freeze-trapping of a Fe-peroxo species after treatment with H2O2 by a specific strengthening of the Fe-O bond, spectroscopic mutant analysis, overview Desulfarculus baarsii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.15.1.2 additional information
-
additional information kinetics, resonance Raman spectroscopy Desulfarculus baarsii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+ the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination Desulfarculus baarsii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + H+ Desulfarculus baarsii the enzyme catalyzes the one-electron reduction of O2 to H2O2, providing an antioxidant defense in some bacteria rubredoxin + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Desulfarculus baarsii Q46495 gene sor
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination, the reaction procedes via a Fe3+-peroxo intermediate Desulfarculus baarsii rubredoxin + H2O2
-
?
1.15.1.2 reduced rubredoxin + superoxide + H+ the enzyme catalyzes the one-electron reduction of O2 to H2O2, providing an antioxidant defense in some bacteria Desulfarculus baarsii rubredoxin + H2O2
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 reduced rubredoxin
-
Desulfarculus baarsii