EC Number |
Cofactor |
Reference |
---|
1.15.1.2 | cytochrome c |
artificial electron carrier |
390148 |
1.15.1.2 | desulforedoxin |
endogenous, contains Zn2+, the protein is able to transfer electrons to superoxide reductase with a maximum kapp of 31/min at an ionic strength of 57 mM, the enzyme complex with superoxide reductase is not detected by chemical shift perturbation |
727313 |
1.15.1.2 | desulforedoxin |
from Desufovibrio gigas, recombinantly expressed |
726902 |
1.15.1.2 | more |
structure of the neelaredoxin center, oxidized and reduced forms, overview |
714326 |
1.15.1.2 | more |
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 |
715670 |
1.15.1.2 | more |
the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview |
714326 |
1.15.1.2 | more |
titration of Zn-rubredoxin with superoxide reductase, overview. NMR competition assay between desulforedoxin and rubredoxin for binding to SOR, overview |
727313 |
1.15.1.2 | reduced rubredoxin |
- |
674937, 684111, 686522, 686523, 687278, 687582, 687820 |
1.15.1.2 | reduced rubredoxin |
a potential Rd binding site is located in the vicinity of the solvent-exposed residues that are close to the iron centre |
686522 |
1.15.1.2 | reduced rubredoxin |
encoded by gene rub |
686522 |