Any feedback?
Literature summary for 1.15.1.2 extracted from
- Understanding the mechanism of superoxide reductase promoted reduction of superoxide (2007), Eur. J. Inorg. Chem., 2007, 29-38.
No PubMed abstract available
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E47A | comparison of wild-type and mutant transient intermdiates | Desulfarculus baarsii |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| acetate | - |
Desulfarculus baarsii |  |
| acetate | - |
Desulfovibrio desulfuricans | |
| acetate | - |
Pyrococcus furiosus | |
| acetate | - |
Treponema palladium | |
| azide | - |
Desulfarculus baarsii | |
| azide | - |
Desulfovibrio desulfuricans | |
| azide | - |
Pyrococcus furiosus | |
| azide | - |
Treponema palladium | |
| cyanide | - |
Desulfarculus baarsii | |
| cyanide | - |
Desulfovibrio desulfuricans | |
| cyanide | - |
Pyrococcus furiosus | |
| cyanide | - |
Treponema palladium | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| Fe2+ | complex formation, kinetics, and electrochemistry, overview | Desulfovibrio desulfuricans | |
| Fe2+ | complex formation, kinetics, and electrochemistry, overview | Treponema palladium | |
| Fe2+ | complex formation, kinetics, and electrochemistry, overview | Pyrococcus furiosus | |
| additional information | binding of synthetic iron ligand complexes, overview | Desulfovibrio desulfuricans | |
| additional information | binding of synthetic iron ligand complexes, overview | Treponema palladium | |
| additional information | binding of synthetic iron ligand complexes, overview | Pyrococcus furiosus | |
| additional information | binding of synthetic iron ligand complexes, overview | Desulfarculus baarsii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| reduced rubredoxin + superoxide + H+ | Desulfovibrio desulfuricans | - |
rubredoxin + H2O2 | - |
? | |
| reduced rubredoxin + superoxide + H+ | Treponema palladium | - |
rubredoxin + H2O2 | - |
? | |
| reduced rubredoxin + superoxide + H+ | Pyrococcus furiosus | - |
rubredoxin + H2O2 | - |
? | |
| reduced rubredoxin + superoxide + H+ | Desulfarculus baarsii | - |
rubredoxin + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Desulfarculus baarsii | Q46495 | - |
- |
| Desulfovibrio desulfuricans | - |
- |
- |
| Pyrococcus furiosus | P82385 | - |
- |
| Treponema palladium | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview | Desulfovibrio desulfuricans | |
| superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview | Treponema palladium | |
| superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview | Pyrococcus furiosus | |
| superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview | Desulfarculus baarsii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview | Desulfovibrio desulfuricans | ? | - |
? | |
| additional information | comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview | Treponema palladium | ? | - |
? | |
| additional information | comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview | Pyrococcus furiosus | ? | - |
? | |
| additional information | comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview | Desulfarculus baarsii | ? | - |
? | |
| reduced rubredoxin + superoxide + H+ | - |
Desulfovibrio desulfuricans | rubredoxin + H2O2 | - |
? | |
| reduced rubredoxin + superoxide + H+ | - |
Treponema palladium | rubredoxin + H2O2 | - |
? | |
| reduced rubredoxin + superoxide + H+ | - |
Pyrococcus furiosus | rubredoxin + H2O2 | - |
? | |
| reduced rubredoxin + superoxide + H+ | - |
Desulfarculus baarsii | rubredoxin + H2O2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SOR | - |
Desulfovibrio desulfuricans |
| SOR | - |
Treponema palladium |
| SOR | - |
Pyrococcus furiosus |
| SOR | - |
Desulfarculus baarsii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| reduced rubredoxin | - |
Desulfovibrio desulfuricans | |
| reduced rubredoxin | - |
Treponema palladium | |
| reduced rubredoxin | - |
Pyrococcus furiosus | |
| reduced rubredoxin | - |
Desulfarculus baarsii |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
