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Literature summary extracted from

  • Yeh, A.P.; Hu, Y.; Jenney, F.E., Jr.; Adams, M.W.W.; Rees, D.C.
    Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states (2000), Biochemistry, 39, 2499-2508.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2
-
 Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.15.1.2 sitting drop vapor diffusion method Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+/Fe3+ each subunit contains a single mononuclear non-heme iron center Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.2 14300
-
 4 * 14300 Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + H+ Pyrococcus furiosus blue non-heme iron enzyme that functions in anaerobic microbes as a defense mechanism against reactive oxygen species by catalyzing the reduction of superoxide to H2O2 oxidized rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Pyrococcus furiosus P82385
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + H+ blue non-heme iron enzyme that functions in anaerobic microbes as a defense mechanism against reactive oxygen species by catalyzing the reduction of superoxide to H2O2 Pyrococcus furiosus oxidized rubredoxin + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 tetramer 4 * 14300 Pyrococcus furiosus