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Literature summary for 1.15.1.2 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
Search for more literature for 1.15.1.2

Cloned(Commentary)

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information detailed kinetic analysis and comparison of mechanism with 1Fe-SOR isoform neelaredoxin. UV/Vis and EPR-spectral analysis Archaeoglobus fulgidus
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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced rubredoxin + superoxide + H+ Archaeoglobus fulgidus
-
 rubredoxin + H2O2
-
 ?

Organism

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

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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
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)

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

Subunits

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

Synonyms

Synonyms Comment Organism
desulfoferrodoxin
-
 Archaeoglobus fulgidus
Dfx
-
 Archaeoglobus fulgidus

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
reduced rubredoxin
-
 Archaeoglobus fulgidus