Ferritin iron core, Actinide uptake by transferrin and ferritin metalloproteins: two EXAFS studies
Résumé
In order to better understand the mechanisms of actinide uptakeby specific biomolecules, it is essential to explore the intramolecular interactions between the cation and the protein binding site.
Although this has long been done for widely investigated transition metals, very few studies have been devoted to
complexation mechanisms of actinides by active chelation sitesof metalloproteins.
In this field, X-ray absorption spectroscopy has been extensively used as a structural and electronic metal cation
probe. The two examples that are presented here are related totwo metalloproteins in charge of iron transport and storage in eukaryote cells: transferrin and ferritin. U(VI)O22+, Np(IV) and Pu(IV) have been selected because of their possible role as contaminant from the geosphere.
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