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Actinide uptake by transferrin and ferritin metalloproteins

Abstract : In order to better understand the mechanisms of actinide uptake by 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 sites of 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 to two 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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https://hal-normandie-univ.archives-ouvertes.fr/hal-02278750
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Submitted on : Wednesday, September 4, 2019 - 3:40:53 PM
Last modification on : Tuesday, September 28, 2021 - 4:38:04 PM

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Christophe den Auwer, I. Llorens, Philippe Moisy, C. Vidaud, F. Goudard, et al.. Actinide uptake by transferrin and ferritin metalloproteins. Radiochimica Acta, R Oldenbourg Verlag GMBH, 2005, 93 (11), ⟨10.1524/ract.2005.93.11.699⟩. ⟨hal-02278750⟩

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