INFLUENCE OF THE SOLVENT ON CATALASE VS. SOD ACTIVITY OF MANGANESE BIOMIMETIC COMPLEXES

C. PALOPOLI; F. FARABOLLINI; A. CAIMI; M. I. OSELLA; ALEJANDRO I. RECIO BALSELLS; S. SIGNORELLA

Granada

Conferencia; Eurobic11; 2012

Universidad de Granada

Manganese catalases (MnCAT) and superoxide dismutases (MnSOD) deplete O2•- and O22- in cells through a ping-pong mechanism involving cyclic oxidation and reduction of the metal cofactor. To disproportionate O2•- and O22- efficiently, the reduction potential of MnSOD and MnCAT is fine-tuned to values much lower than that of the Mn3+(ac)/Mn2+(ac) couple. A number of di- and mononuclear manganese-based complexes has been investigated as low molecular weight catalytic scavengers of H2O2 and O2•-, respectively.[1,2] In this work we evaluated the catalytic activity of mononuclear Mn complexes with the ligands: 1,3-bis(3,5-diX-salicylidenamino)propane (X=Cl or F), 1,3-bis(5- NO2salicylidenamino)propane in different solvents such as methanol (MeOH) acetonitrile (MeCN), dimethyfomamide (DMF) and dimethylsulfoxide (DMSO).