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Literature summary extracted from

  • Brines, L.M.; Kovacs, J.A.
    Understanding the mechanism of superoxide reductase promoted reduction of superoxide (2007), Eur. J. Inorg. Chem., 2007, 29-38.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.2 E47A comparison of wild-type and mutant transient intermdiates Desulfarculus baarsii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.15.1.2 acetate
-
 Desulfarculus baarsii
1.15.1.2 acetate
-
 Desulfovibrio desulfuricans
1.15.1.2 acetate
-
 Pyrococcus furiosus
1.15.1.2 acetate
-
 Treponema palladium
1.15.1.2 azide
-
 Desulfarculus baarsii
1.15.1.2 azide
-
 Desulfovibrio desulfuricans
1.15.1.2 azide
-
 Pyrococcus furiosus
1.15.1.2 azide
-
 Treponema palladium
1.15.1.2 cyanide
-
 Desulfarculus baarsii
1.15.1.2 cyanide
-
 Desulfovibrio desulfuricans
1.15.1.2 cyanide
-
 Pyrococcus furiosus
1.15.1.2 cyanide
-
 Treponema palladium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+ a non-heme, iron-containing enzyme, in the catalytically active reduced state, SORs contain a high-spin FeII center ligated by four equatorial histidine units and one apical cysteinate residue trans to an open site. Additionally, a number of SORs also contain a second rubredoxin-like [Fe(SCys)4] center, complex formation, kinetics, and electrochemistry, overview Desulfarculus baarsii
1.15.1.2 Fe2+ complex formation, kinetics, and electrochemistry, overview Desulfovibrio desulfuricans
1.15.1.2 Fe2+ complex formation, kinetics, and electrochemistry, overview Treponema palladium
1.15.1.2 Fe2+ complex formation, kinetics, and electrochemistry, overview Pyrococcus furiosus
1.15.1.2 additional information binding of synthetic iron ligand complexes, overview Desulfovibrio desulfuricans
1.15.1.2 additional information binding of synthetic iron ligand complexes, overview Treponema palladium
1.15.1.2 additional information binding of synthetic iron ligand complexes, overview Pyrococcus furiosus
1.15.1.2 additional information binding of synthetic iron ligand complexes, 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 reduced rubredoxin + superoxide + H+ Desulfovibrio desulfuricans
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Treponema palladium
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Pyrococcus furiosus
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Desulfarculus baarsii
-
 rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Desulfarculus baarsii Q46495
-
-
1.15.1.2 Desulfovibrio desulfuricans
-
-
-
1.15.1.2 Pyrococcus furiosus P82385
-
-
1.15.1.2 Treponema palladium
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview Desulfovibrio desulfuricans
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview Treponema palladium
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview Pyrococcus furiosus
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview Desulfarculus baarsii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 additional information comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview Desulfovibrio desulfuricans ?
-
 ?
1.15.1.2 additional information comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview Treponema palladium ?
-
 ?
1.15.1.2 additional information comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview Pyrococcus furiosus ?
-
 ?
1.15.1.2 additional information comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview Desulfarculus baarsii ?
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Desulfovibrio desulfuricans rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Treponema palladium rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Pyrococcus furiosus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Desulfarculus baarsii rubredoxin + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 SOR
-
 Desulfovibrio desulfuricans
1.15.1.2 SOR
-
 Treponema palladium
1.15.1.2 SOR
-
 Pyrococcus furiosus
1.15.1.2 SOR
-
 Desulfarculus baarsii

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 reduced rubredoxin
-
 Desulfovibrio desulfuricans
1.15.1.2 reduced rubredoxin
-
 Treponema palladium
1.15.1.2 reduced rubredoxin
-
 Pyrococcus furiosus
1.15.1.2 reduced rubredoxin
-
 Desulfarculus baarsii