1.13.11.6	1,10-phenanthroline	Fe2+ chelator, 1 mM, complete inhibition	62	
1.13.11.6	1-ethyl-3-(3-dimethylaminopropyl)carbodiimide methiodide	carboxyl-directed reagent, 1 mM, 26% inhibition	124941	
1.13.11.6	2,2'-dipyridyl	Fe2+ chelator, 1 mM, complete inhibition	375	
1.13.11.6	4,6-dibromo-3-hydroxyanthranilic acid	NCR-631, characterization of in vivo effects, reversible inhibition with short half-life following systematic administration	108352	
1.13.11.6	4-Bromo-3-hydroxyanthranilic acid	competitive	29532	
1.13.11.6	4-Bromo-3-hydroxyanthranilic acid	-	29532	
1.13.11.6	4-Chloro-3-hydroxyanthranilate	the inactivation results in the consumption of 2 equivalents of oxygen and the production of superoxide. The inhibitor stimulates the oxidation of the active site Fe(II) to the catalytically inactive Fe(III) oxidation state. The inactivated enzyme can be reactivated by treatment with DTT and FeI(II). The nhibitor does not form an adduct with the enzyme. Four conserved cysteines are oxidized to two disulfides (Cys125-Cys128 and Cys162-Cys165) during the inactivation reaction. These results are consistent with a mechanism in which the enzyme, complexed to the inhibitor and O2, generates superoxide which subsequently dissociates, leaving the inhibitor and the oxidized iron center at the active site	12364	
1.13.11.6	4-Chloro-3-hydroxyanthranilate	-	12364	
1.13.11.6	4-Chloro-3-hydroxyanthranilate	it is possible that inhibition of 3-HAD may improve neurologic status through an increased production of kynurenic acid, a non-specific inhibitor of excitatory amino acid receptors and an inhibitor of quinolinic acid neurotoxicity	12364	
1.13.11.6	4-Chloro-3-hydroxyanthranilic acid	competitive	43429