EC Number   |
Cofactor |
Reference |
|---|
    1.15.1.2 | reduced rubredoxin |
- |
674937, 684111, 686522, 686523, 687278, 687582, 687820 |
| 1.15.1.2 | rubredoxin |
- |
744022 |
| 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 | cytochrome c |
artificial electron carrier |
390148 |
| 1.15.1.2 | rubredoxin |
assumed to be the phsiological electron carrier |
390148 |
| 1.15.1.2 | rubredoxin |
contains on-heme [Fe(His)4Cys] active sites. Enzymatic reduction of the enzyme iron sites with use of NADH:rubredoxin oxidoreductase and rubredoxin, both from Thermotoga maritima, rates of enzymatic reduction of the ferric center I and enzyme sites are measured |
726989 |
| 1.15.1.2 | reduced rubredoxin |
encoded by gene rub |
686522 |
| 1.15.1.2 | rubredoxin |
endogenous rubredoxin, recombinantly expressed |
726902 |
| 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 | rubredoxin |
endogenous. A monomeric, non-heme iron protein that contains a tetrahedral FeS4 metal center. The rubredoxin surface involved in the electron transfer complex with superoxide reductase comprises the solvent-exposed hydrophobic residues in the vicinity of its metal center, Cys9, Gly10, Cys42, Gly43, and Ala44. Kd of 0.003 mM at 59 mM ionic strength by NMR. Model structure of superoxide reductase-rubredoxin complex, overview |
727313 |
