EC Number   |
Inhibitors |
Structure |
|---|
   1.7.5.1 | 2-n-heptyl-4-hydroxyquinoline N-oxide |
the quinol-dependent, but not the viologen dye dependent, activity is inhibited reversibly by treatment with 2-n-heptyl-4-hydroxyquinoline N-oxide |
   |
| 1.7.5.1 | 2-n-heptyl-4-hydroxyquinoline N-oxide |
- |
|
| 1.7.5.1 | 2-n-heptyl-4-hydroxyquinoline N-oxide |
has significant effects on the reduction kinetics of NarGHIH56R and NarGHIH205Y |
|
| 1.7.5.1 | 2-n-heptyl-4-hydroxyquinoline N-oxide |
quinol-binding-site inhibitor, elicits a much stronger inhibitory effect than stigmatellin on the reoxidation of the hemes |
|
| 1.7.5.1 | azide |
5 mM, 95-98% inhibition |
|
| 1.7.5.1 | cyanide |
1 mM, 95-98% inhibition |
|
| 1.7.5.1 | diethyl dicarbonate |
the quinol-dependent, but not the viologen dye dependent, activity is inhibited irreversibly by exposure to diethyl pyrocarbonate |
|
| 1.7.5.1 | KCN |
1 mM, complete inhibition |
|
| 1.7.5.1 | more |
p-chloromercuribenzoate (0.5 mM) or 2-heptyl-4-hydroxyquinolin N-oxide (1 mM) are almost without effect on the purified enzyme tested with reduced viologen as electron donor |
|
| 1.7.5.1 | NaN3 |
10 mM, complete inhibition |
|
