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Literature summary extracted from

  • Rodrigues, J.V.; Saraiva, L.M.; Abreu, I.A.; Teixeira, M.; Cabelli, D.E.
    Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: comparison with neelaredoxin (2007), J. Biol. Inorg. Chem., 12, 248-256.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 expression of Dfx in Escherichia coli strain BL21 Archaeoglobus fulgidus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.15.1.2 additional information
-
 additional information detailed kinetic analysis and comparison of mechanism with 1Fe-SOR isoform neelaredoxin. UV/Vis and EPR-spectral analysis Archaeoglobus fulgidus
1.15.1.2 additional information
-
 additional information rapid kinetics measurements and pH-dependence, stopped-flow kinetics of electron transfer between rubredoxin and desulfoferrodoxin, overview Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+ a nonheme iron-containing enzyme, 2Fe-SOR or desulfoferrodoxin class of superoxide reductases Archaeoglobus fulgidus
1.15.1.2 Iron 2.3 atoms per subunit Archaeoglobus fulgidus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.2 15000
-
 2 * 15000, SDS-PAGE Archaeoglobus fulgidus
1.15.1.2 30000
-
 gel filtration Archaeoglobus fulgidus

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+ Archaeoglobus fulgidus
-
 rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Archaeoglobus fulgidus
-
 isoform 2Fe-SOR, comparison of mechanism with 1Fe-SOR isoform neelaredoxin
-
1.15.1.2 Archaeoglobus fulgidus O29903
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.2 recombinant Dfx from Escherichia coli strain BL21 by anion exchange chromatography, ultrafiltration, and gel filtration Archaeoglobus fulgidus
1.15.1.2 recombinant enzyme Archaeoglobus fulgidus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin the initial reaction involves the formation of a short-lived transient that decays by a proton-dependent step. This process generates an Fe3+–OH species, which is converted to a glutamate-bound one. The function of center I of Dfx remains to be elucidated. The completion of the catalytic cycle of SOR, which involves the re-reduction of the active site, can be attained by reduced rubredoxin Archaeoglobus fulgidus
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, the active center of SORs consists of a ferrous ion coordinated by four histidines and one cysteine in a square-pyramidal geometry, formation of a hydroxo-iron ligated species upon the decay of the first transient species followed by conversion to the final species upon binding of the glutamate sixth ligand, phosphate can serve as an exogenous sixth ligand, overview Archaeoglobus fulgidus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Archaeoglobus fulgidus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ SORs are nonheme iron-containing enzymes that remove superoxide by reducing it to hydrogen peroxide Archaeoglobus fulgidus rubredoxin + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 dimer 2 * 15000, SDS-PAGE Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 desulfoferrodoxin
-
 Archaeoglobus fulgidus
1.15.1.2 Dfx
-
 Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.15.1.2 7
-
 assay at Archaeoglobus fulgidus

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 reduced rubredoxin
-
 Archaeoglobus fulgidus