EC Number |
Cofactor |
Reference |
---|
1.15.1.2 | cytochrome c |
artificial electron carrier |
390148 |
1.15.1.2 | rubredoxin |
assumed to be the phsiological electron carrier |
390148 |
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 |
1.15.1.2 | reduced rubredoxin |
rubredoxin is reduced by ferredoxin:NADP+ reductase from spinach and NADPH |
686751 |
1.15.1.2 | more |
structure of the neelaredoxin center, oxidized and reduced forms, overview |
714326 |
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 |
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 | desulforedoxin |
from Desufovibrio gigas, recombinantly expressed |
726902 |