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Literature summary for 1.15.1.2 extracted from
- Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site (2011), J. Biol. Inorg. Chem., 16, 889-898.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant SORs, and of rubredoxin in Escherichia coli strain BL21(DE3) | Desulfarculus baarsii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C13S | site-directed mutagenesis, the lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide | Desulfarculus baarsii |
| Y115A | site-directed mutagenesis, the Y115A SOR mutant folds properly, this mutation does not affect the general properties of the two iron sites of SOR | Desulfarculus baarsii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | stopped-flow kinetic analysis, overview | Desulfarculus baarsii |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe | 2Fe-SOR contains iron center I and iron center II, function of iron center I as an electronic relay between a reductase enzyme and iron center II, overview. The active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, which functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction | Desulfarculus baarsii |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Desulfarculus baarsii | in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview | ? | - |
? | |
| reduced rubredoxin + superoxide + 2 H+ | Desulfarculus baarsii | - |
rubredoxin + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Desulfarculus baarsii | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant SORs, and rubredoxin from Escherichia coli strain BL21(DE3) to homogeneity by anion exchange chromatography and gel filtration | Desulfarculus baarsii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview | Desulfarculus baarsii | ? | - |
? | |
| additional information | artificial reduction of the SOR iron active site using the NADPH:flavodoxin oxidoreductase from Escherichia coli | Desulfarculus baarsii | ? | - |
? | |
| reduced rubredoxin + superoxide + 2 H+ | - |
Desulfarculus baarsii | rubredoxin + H2O2 | - |
? | |
| reduced rubredoxin + superoxide + 2 H+ | the mononuclear iron center with an FeN4S1 coordination catalyzes the one electron reduction of superoxide to form hydrogen peroxide in presence of an additional rubredoxin-like desulforedoxin iron center | Desulfarculus baarsii | rubredoxin + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | three-dimensional structure of the homodimeric SOR, modelling, overview | Desulfarculus baarsii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SOR | - |
Desulfarculus baarsii |
| superoxide reductase | - |
Desulfarculus baarsii |
| two-iron superoxide reductase | - |
Desulfarculus baarsii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Desulfarculus baarsii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Desulfarculus baarsii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, that functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction | Desulfarculus baarsii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the SOR active site is located at the surface of the protein and consists of a mononuclear iron center, named center II, pentacoordinated in its ferrous state by four nitrogen atoms from histidine residues in an equatorial plane and one sulfur atom from a cysteine residue in an axial position. It displays a high redox potential. The lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide | Desulfarculus baarsii |
| physiological function | superoxide reductase, SOR, is a superoxide detoxification system, with a role of the rubredoxin-like iron center in the superoxide detoxifying activity of SOR, overview | Desulfarculus baarsii |
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Release 2023.1 (January 2023)
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