Michaël Carboni
A biomimetic approach to study Iron-Manganese enzymes
Published on 23 September 2011
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Thesis presented September 23, 2011
Abstract:
Nonheme enzymes possessing a dinuclear active site are performing many essential functions such as RiboNucleotide Reductase (RNR) in DNA production and Methane oxygenation (MMO) to convert gas toxic methane in combustible methanol. While most of these enzymes have been shown to possess a diiron active site, new members of this protein family were recently isolated from bacteria and found to possess instead a hetero-dinuclear Fe-Mn active site. The chemical potential of the heterodinuclear metal site is just starting to be evaluated, but available data suggest that it may have capabilities for similarly versatile chemistry as the extensively studied diiron-carboxylate cofactor. In recent years, the study of models based on simple dinuclear metal complexes has became an important tool for gaining insight into the biological functions of such bimetallic cores. The design of binucleating ligands capable of providing asymmetric dinuclear complexes is a subject of great interest. We propose to synthesize dinuclear Fe-Mn complexes to investigate the reactivity and the electronic properties of this new active site. By combining spectroscopic and electronical studies we have gain a better understanding on the reactivity of this new enzymatic system.
Keywords:
Bioinorganic chemistry, Iron-manganese complexes, Mössbauer spectroscopy, EPR spectroscopy, iron-manganese enzymes
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