AI Article Synopsis
- Plutonium's strong radiotoxicity and role in the nuclear industry make it a key focus for understanding internal contamination risks.
- The study aimed to explore how plutonium (Pu(IV)) interacts with calmodulin, a common protein in cells, by examining its complexation with the EF-hand motif.
- Using visible and X-ray absorption spectroscopies, researchers identified three different plutonium species at physiological pH, including 1:1 complexes with calmodulin and other significant formations.
Article Abstract
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.
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| http://dx.doi.org/10.1021/acs.inorgchem.3c00845 | DOI Listing |
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