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Spectroscopic and electrochemical studies of novel model compounds for cytochrome c oxidase
Authors:Kalliopi Ladomenou  Georgios Charalambidis
Institution:a Department of Chemistry, University of Crete, Laboratory of Bioinorganic Chemistry, Voutes Campus, P.O. Box 2208, 71003 Heraklion, Crete, Greece
b Department of Human Nutrition and Dietetics, Technological Educational Institute (TEI) of Crete, I. Kondylaki 46 Street, 723 00 Siteia, Crete, Greece
Abstract:Different metalated porphyrin compounds were studied as model complexes for cytochrome c oxidase. All models contain a tyrosine molecule and a copper binding site. Two of the compounds are bearing an axial pyridine ligand that could possibly coordinate with Fe porphyrins. All complexes were studied using NMR and UV-Vis spectroscopies and it was found that the coordination of the axial ligand is possible only in one of the porphyrins. Moreover, the synthesized catalysts were studied as promising enzyme mimics using a rotating disc electrode in the presence of molecular oxygen.
Keywords:Enzyme models  Porphyrins  Oxidase  Dioxygen  Metalloenzymes
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