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Literature summary for 1.15.1.2 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
Search for more literature for 1.15.1.2

Protein Variants

Protein Variants Comment Organism
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
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

Metals/Ions Comment Organism Structure
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)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
SOR
-
 Desulfarculus baarsii

Cofactor

Cofactor Comment Organism Structure
rubredoxin
-
 Desulfarculus baarsii

General Information

General Information Comment Organism
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
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
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