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Multimetal sites in proteins and enzymes

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 aldehyde oxidoreductase, and the characterization of the multihaem proteins formate dehydrogenase and nitrite reductase. Synthetic analogues for the active sites of dinuclear 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.

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