Catalase is one of the most efficient antioxidants metalloenzymes in biology, responsible for the decomposition of hydrogen peroxide into water and oxygen. The desired antioxidant activity of catalase for medical and industrial applications has inspired the study of metal-based mimics of catalase activity. However, very few of these studies explored water-soluble, non-heme iron-based mimics, the mechanism of action and the impact of the metal center environment on the activity of the complex. Therefore, the first goal of the current work was to investigate pyridine containing macrocyclic Fe (III) complex (L1) as catalase mimic. Mass spectrometry and UV-visible spectrophotometry were used to follow the mechanistic activity of FeL1. The second goal was to evaluate the impact of adjusting the electronic properties (L2 and L3) and the structural rigidity (L1 and L4) of the ligand on the activity of the complex. Cyclic voltammetry, X-ray structural analysis, potentiometric titrations, and UV-visible spectrophotometry were conducted to characterize and study the properties of all the complexes. Kinetic studies, using the method of initial rates, and determination of TON were conducted to compare the activity of the ligands explored.

Catalase cctivity of Fe(III) pyridinophane complexes

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