EC Number   |
Inhibitors |
Structure |
|---|
    1.7.7.1 | N-acetylsuccinimide |
specifically inhibits the ferredoxin binding ability of the enzyme by modifying lysine residues |
   |
| 1.7.7.1 | N-acetylsuccinimide |
loss of enzymatic activity when reduced ferredoxin serves as electron donor, but very little effect with methyl viologen as electron donor, ferredoxin protects the enzyme |
|
| 1.7.7.1 | N-bromosuccinimide |
incubation for 8 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity without effect on substrate binding or other enzyme activities, complex formation with ferredoxin protects the enzyme against inhibition |
|
| 1.7.7.1 | N-bromosuccinimide |
incubation for 8 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity without effect on substrate binding or other enzyme activities, complex formation with ferredoxin protects the enzyme against inhibition; modifies tryptophane and cysteine residues, incubation for 8 hours with 8-fold excess of NBS leads to 50% inhibition of the catalytic activity, incubation for 16 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity |
|
| 1.7.7.1 | N-ethylmaleimide |
47% inhibition at 1 mM |
|
| 1.7.7.1 | NaN3 |
slight |
|
| 1.7.7.1 | o-phenanthroline |
15% inhibition at 5 mM |
|
| 1.7.7.1 | p-chloromercuribenzoate |
- |
|
| 1.7.7.1 | p-chloromercuribenzoate |
nitrite partially protects the inhibition |
|
| 1.7.7.1 | p-chloromercuribenzoate |
complete inhibition at 0.1 mM |
|
