KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic analysis, binding parameters, and electrochemic parameters of the enzyme and Fe2+ complexes, overview | Pyrococcus furiosus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | 1Fe SOR is a non-heme iron enzyme, iron binding and reaction mechanism, detailed overview | Pyrococcus furiosus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced rubredoxin + superoxide + H+ | Pyrococcus furiosus | - |
rubredoxin + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | P82385 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism of SOR involving transfer of an electron and two protons to superoxide to form hydrogen peroxide, kinetic mechanism, detailed overview | Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced rubredoxin + superoxide + H+ | - |
Pyrococcus furiosus | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | SOR is a non-heme iron enzyme that reduces superoxide to peroxide at a diffusion-controlled rate, thiolate acts as a covalent anionic ligand. Replacing the thiolate with a neutral noncovalent ligand makes protonation very endothermic and greatly raises the reduction potential,overview | Pyrococcus furiosus | rubredoxin + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
1Fe SOR | - |
Pyrococcus furiosus |
SOR | - |
Pyrococcus furiosus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
reduced rubredoxin | - |
Pyrococcus furiosus |