EC Number   |
Protein Variants |
Reference |
|---|
    1.7.2.1 | A191E |
slight increase in electron transfer rate constant |
659425 |
| 1.7.2.1 | A191E/G198E |
3fold increase in electron transfer rate constant |
659425 |
| 1.7.2.1 | A83D |
slight increase in electron transfer rate constant |
659425 |
| 1.7.2.1 | A83D/A191E |
3fold increase in electron transfer rate constant |
659425 |
| 1.7.2.1 | A83D/A191E/G198E |
4.7fold increase in electron transfer rate constant |
659425 |
| 1.7.2.1 | A83D/G198E |
3fold increase in electron transfer rate constant |
659425 |
| 1.7.2.1 | C114A |
lacks the type I copper ion in the N-terminal domain, shows catalytic activity |
-, 657476 |
| 1.7.2.1 | C130A |
inactive mutant enzyme, the loss of activity in this mutant is due to the absence of T1Cu and loss of the CuCys130Sg bond rather than any change to the protein structure in this region |
675349 |
| 1.7.2.1 | C135A |
in the anaerobic synchrotron-radiation crystallography structure with peroxide bound to the type 2 copper atom, the peroxide molecule is mainly observed in a side-on binding manner, with a possible minor end-on conformation |
763848 |
| 1.7.2.1 | C135A |
mutant structure analysis, nitrite bound to the T2 Cu site in the eta1-O end-on form, structure analysis, PDB ID 3WKP |
-, 741932 |
