Literature summary for 1.15.1.2 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Pyrococcus furiosus

Crystallization (Commentary)

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	P82385	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Subunits	Comment	Organism
tetramer	4 * 14300	Pyrococcus furiosus

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Release 2023.1 (January 2023)