Comparition of redox potencial and Superoxide Dismutase Activity of Biomimetics Dinuclear Cu2 or Cu/Zn Complexes.

PATRIARCA MATIAS; SIGNORELLA, SANDRA; DAIER, VERÓNICA

CHASCOMUS

Congreso; 4th Latin American Meeting on Biological Inorganic Chemistry; 2014

The metalloenzymes Superoxide dismutases (SOD) efficiently catalyze the dismutation of superoxide anion (O2-) to hydrogen peroxide and dioxygen. They constitute an important defence system in living organisms against several diseases in which (O2-) appears to play an important role, such us: symptoms of aging, some cancers, and cellular degenerating process promoted by AIDS. Four classes of SODs are known, distinguished by the metal prosthetic group: Cu/Zn, Fe, Mn and Ni. Mammalians have three types of SOD: two Cu/Zn and one mononuclear Mn SOD mitochondrial. The design and synthesis of low molecular weight catalysts that mimic natural enzyme function has potential for use as a human pharmaceutical in the treatment or prevention of cellular diseases1,2. This work is aimed at modelling de active sites of these enzymes through the synthesis of Cu/Zn-SOD mimics complexes and compared the rol of Zn in the catalitic. We describe the synthesis, characterization and determination of SOD activity of differentes Cu/Zn and Cu2 complexes: CuZn(Dien)2Im](ClO4)3?(MeOH) (C1), and Cu2(Dien)2Im(ClO4)3 (C2) its Cu2 analogous; CuZn(Salpn)Cl2 (C3) and Cu2(SalbutO)(ClO4) (C4)