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Literature summary for 1.15.1.2 extracted from

  • Lombard, M.; Houee-Levin, C.; Touati, D.; Fontecave, M.; Niviere, V.
    Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis (2001), Biochemistry, 40, 5032-5040.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E47A mutation has almost no effect on the reaction with superoxide Desulfarculus baarsii
K48I 20-fold lower second-order rate constant for the oxidation of the iron center by superoxide compared to wild-type enzyme, K48 may play a role in directing and stabilizing superoxide to the active site at center II Desulfarculus baarsii

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+/Fe3+
-
Desulfarculus baarsii

Organism

Organism UniProt Comment Textmining
Desulfarculus baarsii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and E47A and K48I mutant enzyme Desulfarculus baarsii

Reaction

Reaction Comment Organism Reaction ID
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin very fast bimolecular reaction of iron center II with superoxide, followed by the formation of two successive intermediate species Desulfarculus baarsii

Subunits

Subunits Comment Organism
dimer
-
Desulfarculus baarsii