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Literature summary for 1.15.1.2 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

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

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Archaeoglobus fulgidus
-
Fe-SOR isoform neelaredoxin
-

Reaction

Reaction Comment Organism Reaction ID
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