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Literature summary for 1.15.1.2 extracted from

  • Kovacs, J.A.; Brines, L.M.
    Understanding how the thiolate sulfur contributes to the function of the non-heme iron enzyme superoxide reductase (2007), Acc. Chem. Res., 40, 501-509.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.15.1.2

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a non-heme iron enzyme, isolation of coordinatively unsaturated, mononuclear five coordinate thiolate iron complexes, including [FeIII-(S2Me2N3(Pr,Pr))]+, [FeIII(S2Me2N3-(Et,Pr))]+, and [FeII(SMe2N4(tren))]+ Desulfarculus baarsii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced rubredoxin + superoxide + H+ Desulfarculus baarsii
-
 rubredoxin + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Desulfarculus baarsii Q46495
-
-

Reaction

Reaction Comment Organism Reaction ID
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism, proposed mechanism for SOR-catalyzed reduction of superoxide via hydroperoxo and solvent-bound intermediates, catalytic cycle involving iron complexes, overview Desulfarculus baarsii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information a cysteinate sulfur bound to the iron site, as well as the positioning of the metal ion on the surface versus the interior of the protein, alters the function of Fe-superoxide reductase relative to Fe-superoxide dimutase Desulfarculus baarsii ?
-
 ?
reduced rubredoxin + superoxide + H+
-
 Desulfarculus baarsii rubredoxin + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
Fe-SOR
-
 Desulfarculus baarsii

Cofactor

Cofactor Comment Organism Structure
reduced rubredoxin
-
 Desulfarculus baarsii