Superoxide reductase is an enzyme that catalyzes the conversion of highly reactive and toxic superoxide (O2−) into less toxic hydrogen peroxide (H2O2):
| superoxide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.15.1.2 | ||||||||
| CAS no. | 250679-67-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- reduced rubredoxin + O2− + 2 H+ rubredoxin + H2O2
- Fe2+ + O2− + 2 H+ Fe3++ H2O2
Hydrogen peroxide in turn is reduced to water by rubrerythrin. The 3 substrates of this enzyme are reduced rubredoxin, superoxide, and H+, whereas its two products are rubredoxin and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on superoxide as acceptor (only sub-subclass identified to date). The systematic name of this enzyme class is rubredoxin:superoxide oxidoreductase. Other names in common use include neelaredoxin, and desulfoferrodoxin.
Structural studies
editAs of late 2007[update], 9 structures have been solved for this class of enzymes, with PDB accession codes 1VZG, 1VZH, 1VZI, 1Y07, 2AMU, 2HVB, 2JI1, 2JI2, and 2JI3.
References
editFurther reading
edit- Jenney FE, Verhagen MF, Cui X, Adams MW (1999). "Anaerobic microbes: oxygen detoxification without superoxide dismutase". Science. 286 (5438): 306–9. doi:10.1126/science.286.5438.306. PMID 10514376.
- Yeh AP, Hu Y, Jenney FE, Adams MW, Rees DC (2000). "Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states". Biochemistry. 39 (10): 2499–508. doi:10.1021/bi992428k. PMID 10704199.
- Lombard M, Fontecave M, Touati D, Niviere V (2000). "Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity". J. Biol. Chem. 275 (1): 115–21. arXiv:1412.5038. doi:10.1074/jbc.275.1.115. PMID 10617593. S2CID 7932649.
- Teixeira M; Saraiva, LM; Carita, J; Huber, H; Stetter, KO; Cabelli, D; Teixeira, M (2000). "Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by neelaredoxin". Mol. Microbiol. 38 (2): 322–34. doi:10.1046/j.1365-2958.2000.02121.x. PMID 11069658. S2CID 37827538.
