Abstract: Interaction of Iron (III) complexes of N-Salicylidene-L-amino Acids (i.e., [Fe(sal-L-his)]Cl.H2O and [Fe (sal-L-ala)]Cl.H2O) with catecholate substrate encapsulated in aqueous surfactant micelle has been projected as functional model of dioxygenase enzyme. Biomimetic environment for the study has been provided by the aqueous surfactant medium. Reaction of 3, 5-ditertiarybutyl catechol with the ferric complexes are studied elaborately by electrochemical techniques. These ferric complexes exhibit irreversible redox behaviour in aqueous as well as micellar medium, however, they are found to be quasi-reversible redox process in acetonitrile medium. Interaction of these complexes with 3, 5-ditertiary butyl catechol have shown by the presence of significant redox potential of semiquinone/catechol couple. The redox potential of semiquinone/catechol couple is more positive than that of the redox potential of free 3, 5-ditertiarybutyl catechol, it reflects stabilization of 3, 5-ditertiarybutyl catechol by chelation to ferric centre. Diffusion coefficient values of the catechol coordinated ferric complexes have been calculated and it found to be of the same order as those observed for other one electron reduction processes. The cyclic voltammogram of this interaction have recorded at various scan rates and it showed that this is a diffusion controlled redox process. All these observations provide support to the novel redox active pathway for modeling dioxygenase enzyme to convert phenolic substrates into less harmful aliphatic byproducts.