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superoxide reductase

{{infobox enzyme

| Name = superoxide reductase

| EC_number = 1.15.1.2

| CAS_number = 250679-67-5

| GO_code = 0050605

| image =

| width =

| caption =

}}

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+ \rightleftharpoons rubredoxin + H2O2

:Fe2+ + O2− + 2 H+ \rightleftharpoons 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|alt=As of late 2007}}, 9 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1VZG}}, {{PDB link|1VZH}}, {{PDB link|1VZI}}, {{PDB link|1Y07}}, {{PDB link|2AMU}}, {{PDB link|2HVB}}, {{PDB link|2JI1}}, {{PDB link|2JI2}}, and {{PDB link|2JI3}}.

References

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Further reading

{{refbegin}}

  • {{cite journal | vauthors = Jenney FE, Verhagen MF, Cui X, Adams MW | date = 1999 | title = Anaerobic microbes: oxygen detoxification without superoxide dismutase | journal = Science | volume = 286 | pages = 306–9 | pmid = 10514376 | doi = 10.1126/science.286.5438.306 | issue = 5438 }}
  • {{cite journal | vauthors = Yeh AP, Hu Y, Jenney FE, Adams MW, Rees DC | date = 2000 | title = Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states | journal = Biochemistry | volume = 39 | pages = 2499–508 | pmid = 10704199 | doi = 10.1021/bi992428k | issue = 10 }}
  • {{cite journal | vauthors = Lombard M, Fontecave M, Touati D, Niviere V | date = 2000 | title = Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity | journal = J. Biol. Chem. | volume = 275 | pages = 115–21 | pmid = 10617593 | doi = 10.1074/jbc.275.1.115 | issue = 1 | doi-access = free | arxiv = 1412.5038 | s2cid = 7932649 }}
  • {{cite journal | author = Teixeira M | date = 2000 | title = Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by neelaredoxin | journal = Mol. Microbiol. | volume = 38 | pages = 322–34 | pmid = 11069658 | doi = 10.1046/j.1365-2958.2000.02121.x | last2 = Saraiva | first2 = LM | last3 = Carita | first3 = J | last4 = Huber | first4 = H | last5 = Stetter | first5 = KO | last6 = Cabelli | first6 = D | last7 = Teixeira | first7 = M | issue = 2 | s2cid = 37827538 | doi-access = free }}

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{{Other oxidoreductases}}

{{Enzymes}}

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Category:EC 1.15.1

Category:Enzymes of known structure

{{1.15-enzyme-stub}}