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Literature summary extracted from

  • Bonnot, F.; Tremey, E.; von Stetten, D.; Rat, S.; Duval, S.; Carpentier, P.; Clemancey, M.; Desbois, A.; Niviere, V.
    Formation of high-valent iron-oxo species in superoxide reductase characterization by resonance Raman spectroscopy (2014), Angew. Chem. Int. Ed. Engl., 53, 5926-5930 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.2 I118S site-directed mutagenesis, the mutat shows an altered active site compared to the wild-type and formation of a high-valent iron-oxo species when the mutant protein is reacted with H2O2.. For I118S, formation of the iron-oxo species can also result from the cleavage of the O-O bond of an FeIII-OOH intermediate Desulfarculus baarsii
1.15.1.2 K48I site-directed mutagenesis, the mutat shows an altered active site compared to the wild-type and formation of a high-valent iron-oxo species when the mutant protein is reacted with H2O2. For the K48I mutant, the Fe=O species is formed from the FeIII-OOH species Desulfarculus baarsii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+ SOR is a small non-heme mononuclear iron protein, formation of high-valent iron-oxo species in superoxide reductase, analysis by resonance Raman spectroscopy, overview 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 superoxide + reduced rubredoxin + 2 H+ Desulfarculus baarsii
-
 H2O2 + oxidized rubredoxin
-
 ?
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
-
 H2O2 + oxidized rubredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Desulfarculus baarsii
-
-
-
1.15.1.2 Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 superoxide + reduced rubredoxin + 2 H+
-
 Desulfarculus baarsii H2O2 + oxidized rubredoxin
-
 ?
1.15.1.2 superoxide + reduced rubredoxin + 2 H+
-
 Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14 H2O2 + oxidized rubredoxin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 SOR
-
 Desulfarculus baarsii

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 rubredoxin
-
 Desulfarculus baarsii

General Information

EC Number General Information Comment Organism
1.15.1.2 malfunction mutation of two residues in the second coordination sphere of the SOR iron active site, K48 and I118, leads to the formation of a high-valent iron-oxo species when the mutant proteins are reacted with H2O2 Desulfarculus baarsii
1.15.1.2 additional information the enzyme is used as an unprecedented model to study the mechanisms of O2 activation and of the formation of high-valent iron-oxo species in metalloenzymes. Formation of high-valent iron-oxo species in superoxide reductase, analysis by resonance Raman spectroscopy, overview Desulfarculus baarsii
1.15.1.2 physiological function superoxide reductase (SOR )is a small non-heme iron protein that is not involved in oxidation reactions, but in superoxide radical detoxification in microorganisms Desulfarculus baarsii