Objectif This project aims at making interdisciplinary contribution to the clarification of the role of metal ions at the active sites of several proteins and enzymes containing multimetal sites, particularly those containing iron and copper. The functions of these proteins span the activation and catalytic reactions of small molecules like dioxygen, dihydrogen, inorganic nitrogen and sulphur compounds, and electron transfer processes. The experimental approach involves detailed investigations of the spectroscopic properties of the proteins and several their derivatives, the mechanism of their activities, and the development of small molecule analogues for the multimetal active sites, which is based on intensive biomimetic chemistry on dinuclear and polynuclear complexes with suitable ligands. The latter systems should enable the derivation of structural-spectral, structural-magnetic, and structure-reactivity correlations of extreme importance for protein studies, and the design of new catalytic systems for chemical transformations of substrates of synthetic and environmental interest.Various spectroscopic, kinetic and structural studies performed on the proteins have led to the characterization of various forms of hemocyanins and their tyrosinase like activity, the identification of the substrate binding site of ascorbate oxidase, the complete X-ray and solution structure of desulphuredoxin, the X-ray structure of the molybdenum/iron protein idehyde oxidoreductase, and the characterization of the multihaem proteins formate dehydrogenase and nitrite reductase. Synthetic analogues for the active sites of dinulclear copper and haem-copper proteins have been obtained using polydentate nitrogen ligands, and fuctional models of copper monooxygenase, superoxide dismutase and nitrite reductase enzymes have been developed. Dinuclear iron and manganese complexes with relavance to the non-haem iron proteins and the catalytic centre of photosystem II have also been studied, together with their oxidative activity. The reactivity of peroxynitrite towards a series of metal complexes has been investigated. New theoretical models have been developed to account for the magnetic interaction in dinuclear and polynuclear iron-containing clusters. Champ scientifique natural scienceschemical sciencesinorganic chemistrytransition metalsnatural sciencesbiological sciencesbiochemistrybiomoleculesproteinsenzymes Programme(s) FP3-HCM - Specific research and technological development programme (EEC) in the field of human capital and mobility, 1990-1994 Thème(s) Data not available Appel à propositions Data not available Régime de financement CSC - Cost-sharing contracts Coordinateur UNIVERSITA DEGLI STUDI DI PAVIA Contribution de l’UE Aucune donnée Adresse Via Taramelli, 12 27100 PAVIA Italie Voir sur la carte Coût total Aucune donnée Participants (7) Trier par ordre alphabétique Trier par contribution de l’UE Tout développer Tout réduire CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE France Contribution de l’UE Aucune donnée Adresse Route de Narbonne 205 31077 TOULOUSE Voir sur la carte Coût total Aucune donnée LEIDEN UNIVERSITY Pays-Bas Contribution de l’UE Aucune donnée Adresse 55,Einsteinweg 55 Gorlaeus Laboratoria 2300 RA Leiden Voir sur la carte Coût total Aucune donnée UNIVERSIDADE NOVA DE LISBOA Portugal Contribution de l’UE Aucune donnée Adresse Quinta da Torre 2825 MONTE DA CAPARICA Voir sur la carte Coût total Aucune donnée UNIVERSITY OF CATANIA Italie Contribution de l’UE Aucune donnée Adresse Viale A. Doria 6 95125 Catania Voir sur la carte Coût total Aucune donnée UNIVERSITY OF SOUTHERN DENMARK - UNIVERSITY OF ODENSE Danemark Contribution de l’UE Aucune donnée Adresse 55,Campusvej 55 5230 ODENSE Voir sur la carte Coût total Aucune donnée University of Ioannina Grèce Contribution de l’UE Aucune donnée Adresse 45110 Ioannina Voir sur la carte Coût total Aucune donnée Université de Paris XI (Université Paris-Sud) France Contribution de l’UE Aucune donnée Adresse 91405 Orsay Voir sur la carte Coût total Aucune donnée
