Literature summary extracted from
Mathe, C.; Weill, C.O.; Mattioli, T.A.; Berthomieu, C.; Houee-Levin, C.; Tremey, E.; Niviere, V.
Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii (2007), J. Biol. Chem., 282, 22207-22216.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.15.1.2 |
gene sor, complementation of the Escherichia coli QC2375 mutant strain |
Desulfarculus baarsii |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.15.1.2 |
E114A |
the mutant shows significantly modified pulse radiolysis kinetics for the protonation process of the first reaction intermediate compared to the wild-type enzyme, mutation results in both a strengthening of the S-Fe bond and an increase in the extent of freeze-trapping of a Fe-peroxo species after treatment with H2O2 by a specific strengthening of the Fe-O bond, spectroscopic mutant analysis, overview |
Desulfarculus baarsii |
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.15.1.2 |
additional information |
- |
additional information |
kinetics, resonance Raman spectroscopy |
Desulfarculus baarsii |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.15.1.2 |
Fe2+ |
the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination |
Desulfarculus baarsii |
|
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+ |
Desulfarculus baarsii |
the enzyme catalyzes the one-electron reduction of O2 to H2O2, providing an antioxidant defense in some bacteria |
rubredoxin + H2O2 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.15.1.2 |
Desulfarculus baarsii |
Q46495 |
gene sor |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.15.1.2 |
reduced rubredoxin + superoxide + 2 H+ |
the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination, the reaction procedes via a Fe3+-peroxo intermediate |
Desulfarculus baarsii |
rubredoxin + H2O2 |
- |
? |
|
1.15.1.2 |
reduced rubredoxin + superoxide + H+ |
the enzyme catalyzes the one-electron reduction of O2 to H2O2, providing an antioxidant defense in some bacteria |
Desulfarculus baarsii |
rubredoxin + H2O2 |
- |
? |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.15.1.2 |
reduced rubredoxin |
- |
Desulfarculus baarsii |
|