EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.15.1.2 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.15.1.2 | reduced rubredoxin + superoxide + H+ | Desulfarculus baarsii | - |
rubredoxin + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.15.1.2 | Desulfarculus baarsii | Q46495 | - |
- |
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, proposed mechanism for SOR-catalyzed reduction of superoxide via hydroperoxo and solvent-bound intermediates, catalytic cycle involving iron complexes, overview | Desulfarculus baarsii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.15.1.2 | 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 | ? | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + H+ | - |
Desulfarculus baarsii | rubredoxin + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.15.1.2 | Fe-SOR | - |
Desulfarculus baarsii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.15.1.2 | reduced rubredoxin | - |
Desulfarculus baarsii |