1.7.7.1	additional information	anti-glutamate synthase antibodies recognize nitrite reductase, but inhibit only ferredoxin-linked activity and not methyl viologen-linked activity	2	
1.7.7.1	additional information	potassium chlorate and dithiothreitol are not effective inhibitors	2	
1.7.7.1	EDTA	-	21	
1.7.7.1	p-chloromercuribenzoate	-	43	
1.7.7.1	p-chloromercuribenzoate	nitrite partially protects the inhibition	43	
1.7.7.1	p-chloromercuribenzoate	complete inhibition at 0.1 mM	43	
1.7.7.1	p-chloromercuribenzoate	not	43	
1.7.7.1	N-ethylmaleimide	47% inhibition at 1 mM	49	
1.7.7.1	hydroxylamine	34% inhibition at 10 mM	85	
1.7.7.1	sulfite	-	92	
1.7.7.1	p-hydroxymercuribenzoate	enzyme from higher plants and eukaryotic algae inhibited, cyanobacterial enzyme not	98	
1.7.7.1	p-hydroxymercuribenzoate	-	98	
1.7.7.1	cyanide	-	118	
1.7.7.1	cyanide	92% inhibition at 0.1 mM	118	
1.7.7.1	cyanide	almost complete inhibition from 0.02 mM to 0.2 mM	118	
1.7.7.1	cyanide	competitive inhibition with respect to nitrite	118	
1.7.7.1	cyanide	90% inhibition at 1 mM	118	
1.7.7.1	cyanide	1 mM	118	
1.7.7.1	CO	enzyme from higher plants and algae	176	
1.7.7.1	CO	-	176	
1.7.7.1	CO	forms a complex with the reduced enzyme	176	
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	208	
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	208	
1.7.7.1	azide	-	230	
1.7.7.1	NaN3	slight	238	
1.7.7.1	o-phenanthroline	15% inhibition at 5 mM	239	
1.7.7.1	Phenylglyoxal	inhibits the ability of the enzyme to form a high-affinity complex with ferredoxin by modifying arginine residues	301	
1.7.7.1	Phenylglyoxal	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	301	
1.7.7.1	8-hydroxyquinoline	7% inhibition at 5 mM	321	
1.7.7.1	(NH4)2SO4	slightly inhibitory	399	
1.7.7.1	SO32-	24% inhibition at 10 mM	902	
1.7.7.1	4-hydroxymercuribenzoate	-	970	
1.7.7.1	Mersalyl	-	1982	
1.7.7.1	Mersalyl	reversible by glutathione	1982	
1.7.7.1	bathophenanthroline	slight	2722	
1.7.7.1	pyridoxal-5'-phosphate	75% inhibition of the enzyme with ferredoxin as electron donor after exposure to NaBH4, but no inhibition of the enzyme with methyl viologen as electron donor	4558	
1.7.7.1	N-acetylsuccinimide	specifically inhibits the ferredoxin binding ability of the enzyme by modifying lysine residues	21867	
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	21867	
1.7.7.1	Phenyl mercury acetate	-	94716