Literature summary for 1.15.1.2 extracted from

Lombard, M.; Fontecave, M.; Touati, D.; Niviere, V.
Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity (2000), J. Biol. Chem., 275, 115-121.

Search for more literature for 1.15.1.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Desulfarculus baarsii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+/Fe3+	1.97 iron atoms/subunit, enzyme contains two Fe-centers: center I contains a mononuclear ferric iron coordinated by four cysteines in distorted rubredoxin-type center, center II has a ferrous iron with square pyramidal coordination to four nitrogens from histidines as equatorial ligands and one sulfur from a cysteine as the axial ligand, the reduced form of center II can transfer 1 electron to superoxid anion very efficiently	Desulfarculus baarsii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
14028	-	2 * 14028, ES-MS	Desulfarculus baarsii
27000	-	gel filtration	Desulfarculus baarsii

Organism

Organism	UniProt	Comment	Textmining
Desulfarculus baarsii	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme, gel filtration, anion exchange	Desulfarculus baarsii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
reduced cytochrome c + superoxide + H+	enzyme shows only very weak superoxide dismutase activity	Desulfarculus baarsii	cytochrome c + H2O2	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 14028, ES-MS	Desulfarculus baarsii

Synonyms

Synonyms	Comment	Organism
desulfoferrodoxin	-	Desulfarculus baarsii

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Release 2023.1 (January 2023)