Prof.Dr. W. (fred) Hagen

dr. P.L. (Peter-Leon) Hagedoorn


Life requires some 20 odd elements, and many biocatalysts mandatorily need metal ions for their biological activity. Since present-day life is the product of evolution one can legitimately ask the question: why does a cell go for a particular chemistry. In this framework we are interested in structure-mechanism relations of metalloproteins, in particular metalloenzymes, as biological coordination complexes in a variety of environments. We go after high space-time resolution in the characterization of atomic structural changes on a pre-steady state scale. We have a preference for redox-active transition ions with their spectroscopically interesting colors and magnetic properties. To illustrate this quest the picture zooms in into the structure of a hyperthermophilic ferritin where hard Lewis acid side groups collaborate with a radical-forming tyrosine to catalytically oxidize essential iron ions en route to storage in an intra-protein cavity. We also employ and modify metalloproteins with a view to putative industrial or medical applications. The ferritin is for example usable in water purification.

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