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Literature summary extracted from

  • Rodrigues, J.V.; Abreu, I.A.; Cabelli, D.; Teixeira, M.
    Superoxide reduction mechanism of Archaeoglobus fulgidus one-iron superoxide reductase (2006), Biochemistry, 45, 9266-9278.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.2 E12Q mutation in corrdination site of iron. Detailed kinetic analysis Archaeoglobus fulgidus
1.15.1.2 E12V mutation in corrdination site of iron. Detailed kinetic analysis Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Iron 0.8 atoms per subunit for wild-type, mutant E12V, 1.2 atoms per subunit, mutant E12Q, 0.9 atoms per subunit Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Archaeoglobus fulgidus
-
 Fe-SOR isoform neelaredoxin
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin the initial reaction between O2- and Archaeoglobus fulgidus neelaredoxin leads to a short-lived transient that immediately disappears to yield a solvent-bound ferric species in acid-base equilibrium. The final step corresponds to the slow binding of the glutamate sixth ligand to the oxidized iron, a process that may be bypassed during in vivo catalytic turnover of the enzyme Archaeoglobus fulgidus
a