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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 expression in Escherichia coli Desulfarculus baarsii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.2 14028
-
 2 * 14028, ES-MS Desulfarculus baarsii
1.15.1.2 27000
-
 gel filtration Desulfarculus baarsii

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Desulfarculus baarsii
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 desulfoferrodoxin
-
 Desulfarculus baarsii