Superoxide reductase
From Wikipedia, the free encyclopedia
In enzymology, a superoxide reductase (EC 1.15.1.2) is an enzyme that catalyzes the chemical reaction
- reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
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 accepto acting on superoxide as acceptor (only sub-subclass identified t date). The systematic name of this enzyme class is rubredoxin:superoxide oxidoreductase. Other names in common use include neelaredoxin, and desulfoferrodoxin.
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[edit] 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.
[edit] References
- IUBMB entry for 1.15.1.2
- BRENDA references for 1.15.1.2 (Recommended.)
- PubMed references for 1.15.1.2
- PubMed Central references for 1.15.1.2
- Google Scholar references for 1.15.1.2
- Jenney FE Jr, Verhagen MF, Cui X, Adams MW (1999). "Anaerobic microbes: oxygen detoxification without superoxide dismutase". Science. 286: 306–9. doi:. PMID 10514376.
- Yeh AP, Hu Y, Jenney FE Jr, Adams MW, Rees DC (2000). "Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states". Biochemistry. 39: 2499–508. doi:. 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: 115–21. doi:. PMID 10617593.
- Teixeira M (2000). "Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by neelaredoxin". Mol. Microbiol. 38: 322–34. doi:. PMID 11069658.

