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Journal articles
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.
https://hal-normandie-univ.archives-ouvertes.fr/hal-02278750
Contributor : Cécile Barbot Connect in order to contact the contributor
Submitted on : Wednesday, September 4, 2019 - 3:40:53 PM
Last modification on : Tuesday, September 28, 2021 - 4:38:04 PM
Contributor : Cécile Barbot Connect in order to contact the contributor
Submitted on : Wednesday, September 4, 2019 - 3:40:53 PM
Last modification on : Tuesday, September 28, 2021 - 4:38:04 PM
