A series of mononuclear iron(III) complexes with containing phenolate donor of substituted-salicylaldimine based ligands [Fe(L 1 )(TCC)]·CH 3 OH (1), [Fe(L 2 )(TCC)]·CH 3 OH (2), [Fe(L 3 )(TCC)] (3), and [Fe(L 4 )(TCC)] (4) have been prepared and studied as functional models for catechol dioxygenases (H 2 TCC=tetrachlorocatechol, or HL 1 =N′-(salicylaldimine)-N,N-diethyldiethylenetriamine, HL 2 =N′-(5-Br-salicylaldimine)-N,N-diethyldiethylenetriamine, HL 3 =N′-(4,6-dimethoxy-salycyl-aldimine)-N,N-diethyl-diethylenetriamine, HL 4 =N′-(4-methoxy-salicylaldimine)-N,N-diethyl-diethylenetriamine). They are structural models for inhibitors of enzyme-substrate adducts from the reactions of catechol 1,2-dioxygenases. Complexes 1–4 were characterized by spectroscopic methods and X-ray crystal structural analysis. The coordination sphere of Fe(III) atom of 1–4 is distorted octahedral with N 3 O 3 donor set from the ligand and the substrate TCC occupying cis position, and Fe(III) is in high-spin (S=5/2) electronic ground state. The in situ prepared iron(III) complexes without TCC, [Fe(L 1 )Cl 2 ], [Fe(L 2 )Cl 2 ], [Fe(L 3 )Cl 2 ], and [Fe(L 4 )Cl 2 ] are reactive towards intradiol cleavage of the 3,5-di-tert-butylcatechol (H 2 DBC) in the presence of O 2 or air. The reaction rate of catechol 1,2-dioxygenase depends on the redox potential and acidity of iron(III) ions in complexes as well as the substituent effect of the ligands. We have identified the reaction products and proposed the mechanism of the reactions of these iron(III) complexes with H 2 DBC with O 2 .