Search results for "CARBONYLATION"
showing 2 items of 72 documents
Protein oxidation in metabolic syndrome
2013
Purpose: Oxidative stress plays a pivotal role in the pathogenesis of the metabolic syndrome and in the progression of its complications. Carbonylated proteins are a stable marker of severe oxidative stress because damage to the protein structure is irreversible and may cause an inhibition of their enzymatic activity or an increased susceptibility to proteolysis. There are few data regarding protein oxidation in metabolic syndrome, although elevated levels of carbonyl groups are often detected in subjects with obesity, diabetes mellitus, hypertension or dyslipidemia, well-known components of the metaboic syndrome. In particular, obesity, insulin resistance and diabetes mellitus are frequent…
Self-assembly of square planar rhodium carbonyl complexes with 4,4-disubstituted-2,2′-bipyridine ligands
2020
The impact of non-covalent interactions and reaction conditions on formation and self-assembly of ionic pairs of Rh complexes with 4,4’-disubstituted bipyridine ligands ([Rh(L1)(CO)2][Rh(CO)2Cl2])n (1), [Rh(L1)2Cl2][Rh(CO)2Cl2] (2), ([Rh(L1)(CO)2][Rh(CO)2Cl2][Rh(L1)(CO)2]n([Rh(CO)2(Cl)2])n) (3), ([Rh(L2)CO2] [Rh(CO)2Cl2])n∙EtOH (4), ([Rh(L2)(CO)2])n ([Rh(CO)2Cl2])n (5) (L1 = 4,4’-dimethyl-2,2’-bipyridine, L2 = 4,4’-diamine-2,2’-bipyridine) have been studied. Packing of square planar Rh complexes favor formation of one-dimensional chains. In structure 1, the polymeric chain is formed by the alternating cationic [Rh(L1)(CO)2]+ and the anionic [Rh(CO)2Cl2]- units leading to a neutral pseudo li…