EC Number   |
Inhibitors |
Structure |
|---|
    1.7.7.1 | more |
anti-glutamate synthase antibodies recognize nitrite reductase, but inhibit only ferredoxin-linked activity and not methyl viologen-linked activity |
 |
| 1.7.7.1 | cyanide |
competitive inhibition with respect to nitrite |
  |
| 1.7.7.1 | p-chloromercuribenzoate |
complete inhibition at 0.1 mM |
|
| 1.7.7.1 | CO |
enzyme from higher plants and algae |
|
| 1.7.7.1 | p-hydroxymercuribenzoate |
enzyme from higher plants and eukaryotic algae inhibited, cyanobacterial enzyme not |
|
| 1.7.7.1 | CO |
forms a complex with the reduced 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 | Phenylglyoxal |
inhibits the ability of the enzyme to form a high-affinity complex with ferredoxin by modifying arginine 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 |
|
