Due
to its presence in the nuclear industry and its strong
radiotoxicity,
plutonium is an actinide of major interest in the event of internal
contamination. To improve the understanding of its mechanisms of transport
and accumulation in the body, the complexation of Pu(IV) to the most
common protein calcium-binding motif found in cells, the EF-hand motif
of calmodulin, was investigated. Visible and X-ray absorption spectroscopies
(XAS) in solution made it possible to investigate the speciation of
plutonium at physiological pH (pH 7.4) and pH 6 in two variants of
the calmodulin Ca-binding site I and using Pu(IV) in different media:
carbonate, chloride, or nitrate solutions. Three different species
of Pu were identified in the samples, with formation of 1:1 Pu(IV):calmodulin
peptide complexes, Pu(IV) reduction, and formation of peptide-mediated
Pu(IV) hexanuclear cluster.