EC Number   |
General Information |
Reference  |
|---|
    1.15.1.2 | physiological function |
superoxide reductases play a key role in defence mechanisms against toxic oxygen species. SOR is responsible for scavenging toxic superoxide anion radicals, catalysing the one-electron reduction of superoxide to hydrogen peroxide |
713639 |
| 1.15.1.2 | more |
SORs can be classified as 1Fe-SORs, or neelaredoxins, or as 2Fe-SORs, or desulfoferrodoxins, according to the number of metal centres. Both share a common active site in which the reduction of superoxide anion occurs. This site is composed of a pentacoordinated iron with four equatorial histidine imidazoles and one axial cysteine sulfur in a square-pyramidal geometry [Fe(Cys)(His)4] |
713642 |
| 1.15.1.2 | physiological function |
the neelaredoxin-type SOR keeps toxic oxygen species levels under control. SORs are involved in scavenging superoxide radicals from the cell by catalyzing the reduction of superoxide to hydrogen peroxide |
713642 |
| 1.15.1.2 | physiological function |
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system |
-, 714326 |
| 1.15.1.2 | physiological function |
SOR is responsible for reductive eliminatioon of toxic superoxide as part of the detoxifying system |
714326 |
| 1.15.1.2 | physiological function |
superoxide reductase is involved in superoxide detoxification |
714327 |
| 1.15.1.2 | more |
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 |
715670 |
| 1.15.1.2 | 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 |
715670 |
| 1.15.1.2 | evolution |
the enzyme belongs to the class I superoxide reductase family |
-, 726902 |
| 1.15.1.2 | more |
direct electron transfer measurements, in the presence of superoxide anion, overview |
-, 726902 |
