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Control of stability and reactivity of dioxygen-binding in dinuclear biomimetic copper compounds


Research objectives and content
The aim of the bioinorganic chemistry is to define model systems. Those models systems are intended to imitate the natural functions of fewer proteins while avoiding the difficulties introduced in the study of the naturals systems by the great size of the large proteins. The research project is proposed towards better understanding of dioxygen binding to biomimetic copper complexes and their application in catalytic oxidation reactions. Proteins containing cooper ions at the active site are principally involved as redox-catalysts in a range of biological processes, such as electron transfer, dioxygen transport. Their coordination complexes are excellent candidates for biometics studies. A first example of dioxygen binding and stabilization of a metal-dioxygen adduct at room temperature in a polar solvent was published by the Leiden Laboratory. Proteins like hemocyanin are able to bind and activate dioxygen at room temperature and in aqueous conditions. The next step in the project deals with the simultaneous study of the electronics effects on the redox potential of Cu compounds (modifying the ligands environments), the steric control of the coordination site and the control of the entropic term to the instability of the dioxygen complex. And also to study the reactivity of the compounds towards an external substrate that is to be oxidized. Tralning content (objective. benefit and expected impact)
This research project will allow me to extend my knowledge to the field of bioinorganic chemistry, to gain a more specific experience in the field of heterocyclic ligands synthesis and above all to acquire a good training in the analytical techniques.
Links with industry / industrial relevance (22)

Funding Scheme

RGI - Research grants (individual fellowships)


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