STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS

The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.

Antioxidant activity of tetra nitrosyl iron complex with thiosulfate ligands and its effect on catalytic activity of mitochondrial enzymes in vitro

The antioxidant and antiradical properties of the tetra nitrosyl iron complex with thiosulfate ligands (TNIC) in the mouse brain homogenates in vitro were also studied. It was found for the first time that TNIC is an effective antioxidant. The effect of TNIC on the catalytic activity of mitochondrial enzymes: cytochrome c oxidase and monoamine oxidase A has been studied. It was shown for the first time that TNIC is an inhibitor of the catalytic activity of cytochrome c oxidase and monoamine oxidase A in the brain mitochondria isolated from animals in vitro.

Superstructured metallocorroles for electrochemical CO2 reduction

The (nitrosyl)iron complex of the corrole with a proximal tyrosine-like proton relay moiety is a potent catalyst for the electro-reduction of CO2 to CO.