Biology:Superoxide reductase

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superoxide reductase
Identifiers
EC number1.15.1.2
CAS number250679-67-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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+ [math]\displaystyle{ \rightleftharpoons }[/math] rubredoxin + H2O2
Fe2+ + O2 + 2 H+ [math]\displaystyle{ \rightleftharpoons }[/math] 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 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

  • "Anaerobic microbes: oxygen detoxification without superoxide dismutase". Science 286 (5438): 306–9. 1999. doi:10.1126/science.286.5438.306. PMID 10514376. 
  • "Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states". Biochemistry 39 (10): 2499–508. 2000. doi:10.1021/bi992428k. PMID 10704199. 
  • "Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity". J. Biol. Chem. 275 (1): 115–21. 2000. doi:10.1074/jbc.275.1.115. PMID 10617593. 
  • 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.