EC Number   |
Protein Variants |
Reference |
|---|
   1.8.2.2 | C123G |
residue probably acts as sixth distal axial ligand of a heme iron, mutant is inactive |
-, 724861 |
| 1.8.2.2 | C138H |
inactive |
765056 |
| 1.8.2.2 | C138M |
inactive |
765056 |
| 1.8.2.2 | C96G |
site-directed mutagenesis, inactive mutant |
742887 |
| 1.8.2.2 | C96H |
site-directed mutagenesis, inactive mutant |
742887 |
| 1.8.2.2 | C96M |
site-directed mutagenesis, inactive mutant |
742887 |
| 1.8.2.2 | K208G |
site-directed mutagenesis, the mutant is catalytically active in thiosulfate oxidation as well as in tetrathionate reduction |
742887 |
| 1.8.2.2 | K208N |
site-directed mutagenesis, the mutant is catalytically active in thiosulfate oxidation as well as in tetrathionate reduction |
742887 |
| 1.8.2.2 | M209G |
site-directed mutagenesis, the mutant is catalytically active in thiosulfate oxidation as well as in tetrathionate reduction |
742887 |
| 1.8.2.2 | more |
construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains |
-, 742899 |
