Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Bonnot, F.; Duval, S.; Lombard, M.; Valton, J.; Houee-Levin, C.; Niviere, V.
    Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site (2011), J. Biol. Inorg. Chem., 16, 889-898.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 expression of wild-type and mutant SORs, and of rubredoxin in Escherichia coli strain BL21(DE3) Desulfarculus baarsii

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.2 C13S site-directed mutagenesis, the lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide Desulfarculus baarsii
1.15.1.2 Y115A site-directed mutagenesis, the Y115A SOR mutant folds properly, this mutation does not affect the general properties of the two iron sites of SOR 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 stopped-flow kinetic analysis, overview Desulfarculus baarsii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe 2Fe-SOR contains iron center I and iron center II, function of iron center I as an electronic relay between a reductase enzyme and iron center II, overview. The active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, which functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction 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 additional information Desulfarculus baarsii in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview ?
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Desulfarculus baarsii
-
 rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Desulfarculus baarsii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.2 recombinant wild-type and mutant SORs, and rubredoxin from Escherichia coli strain BL21(DE3) to homogeneity by anion exchange chromatography and gel filtration Desulfarculus baarsii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 additional information in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview Desulfarculus baarsii ?
-
 ?
1.15.1.2 additional information artificial reduction of the SOR iron active site using the NADPH:flavodoxin oxidoreductase from Escherichia coli Desulfarculus baarsii ?
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Desulfarculus baarsii rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ the mononuclear iron center with an FeN4S1 coordination catalyzes the one electron reduction of superoxide to form hydrogen peroxide in presence of an additional rubredoxin-like desulforedoxin iron center Desulfarculus baarsii rubredoxin + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 homodimer three-dimensional structure of the homodimeric SOR, modelling, overview Desulfarculus baarsii

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 SOR
-
 Desulfarculus baarsii
1.15.1.2 superoxide reductase
-
 Desulfarculus baarsii
1.15.1.2 two-iron superoxide reductase
-
 Desulfarculus baarsii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.15.1.2 25
-
 assay at Desulfarculus baarsii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.15.1.2 7.6
-
 assay at Desulfarculus baarsii

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 additional information the active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, that functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction Desulfarculus baarsii

General Information

EC Number General Information Comment Organism
1.15.1.2 additional information the SOR active site is located at the surface of the protein and consists of a mononuclear iron center, named center II, pentacoordinated in its ferrous state by four nitrogen atoms from histidine residues in an equatorial plane and one sulfur atom from a cysteine residue in an axial position. It displays a high redox potential. The lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide Desulfarculus baarsii
1.15.1.2 physiological function superoxide reductase, SOR, is a superoxide detoxification system, with a role of the rubredoxin-like iron center in the superoxide detoxifying activity of SOR, overview Desulfarculus baarsii