Superoxide reductase
Today, we want to talk about Superoxide reductase, a topic that is present in the lives of many people. Superoxide reductase is a broad and relevant topic in today's society, covering aspects ranging from the personal to the global. Many people have been impacted by Superoxide reductase in one way or another, and its influence extends to different areas of daily life. In this article, we will explore the most relevant aspects of Superoxide reductase, analyzing its impact, its importance and the implications it has for our society. Through this analysis, we hope to provide a clearer and deeper insight into Superoxide reductase, and offer valuable information that contributes to the understanding and reflection on this topic.
| 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 | ||||||||
| |||||||||
Superoxide reductase is an enzyme that catalyzes the conversion of highly reactive and toxic superoxide (O2−) into less toxic hydrogen peroxide (H2O2):
- 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
As of late 2007, 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
Further reading
- 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.
