EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    1.15.1.2 | more |
in times of oxidative stress, enzyme efficiently diverts intracellular reducing equivalents to superoxide |
Desulfovibrio vulgaris |
? |
- |
? |
| 1.15.1.2 | more |
enzyme has O2 radical detoxification activity, catalyzed by the SOR-ferrocyanide complex, which does not conduct to the production of the toxic H2O2 species |
Desulfarculus baarsii |
? |
- |
? |
| 1.15.1.2 | more |
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 | more |
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview |
Desulfovibrio desulfuricans |
? |
- |
? |
| 1.15.1.2 | more |
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview |
Treponema palladium |
? |
- |
? |
| 1.15.1.2 | more |
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview |
Pyrococcus furiosus |
? |
- |
? |
| 1.15.1.2 | more |
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview |
Desulfarculus baarsii |
? |
- |
? |
| 1.15.1.2 | more |
structure-function relationship, overview |
Methanothermobacter thermautotrophicus |
? |
- |
? |
| 1.15.1.2 | more |
structure-function relationship, overview |
Desulfovibrio desulfuricans |
? |
- |
? |
| 1.15.1.2 | more |
structure-function relationship, overview |
Megalodesulfovibrio gigas |
? |
- |
? |
