How Does Iron Storage Protein Ferritin Interact with Plutonium (and Thorium)?,Chemistry - A European Journal

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How Does Iron Storage Protein Ferritin Interact with Plutonium (and Thorium)?
Chemistry - A European Journal ( IF 3.9 ) Pub Date : 2020-09-21 , DOI: 10.1002/chem.202003653
Cyril Zurita ₁ , Satoru Tsushima _{2,

3} , Carole Bresson ₄ , Marta Garcia Cortes ₄ , Pier Lorenzo Solari ₅ , Aurélie Jeanson ₁ , Gaëlle Creff ₁ , Christophe Den Auwer ₁

Affiliation

The impact of the contamination of living organisms by actinide elements has been a constant subject of attention since the 1950s. But to date still little is understood. Ferritin is the major storage and regulation protein of iron in many organisms, it consists of a protein ring and a ferrihydric core at the center. This work sheds light on the interactions of early actinides (Th, Pu) at oxidation state +IV with ferritin and its ability to store those elements at physiological pH compared to Fe. The ferritin–thorium load curve suggests that Th^IV saturates the protein (2840 Th atoms per ferritin) in a similar way that Fe does on the protein ring. Complementary spectroscopic techniques (spectrophotometry, infrared spectroscopy, and X‐ray absorption spectroscopy) were combined with molecular dynamics to provide a structural model of the interaction of Th^IV and Pu^IV with ferritin. Comparison of spectroscopic data together with MD calculations suggests that Th^IV and Pu^IV are complexed mainly on the protein ring and not on the ferrihydric core. Indeed from XAS data, there is no evidence of Fe neighbors in the Th and Pu environments. On the other hand, carboxylates from amino acids of the protein ring and a possible additional carbonate anion are shaping the cation coordination spheres. This thorough description from a molecular view point of Th^IV and Pu^IV interaction with ferritin, an essential iron storage protein, is a cornerstone in comprehensive nuclear toxicology.

中文翻译：

铁存储蛋白铁蛋白如何与P（和Thor）相互作用？

自1950年代以来，act系元素对生物的污染就一直是人们关注的焦点。但是到目前为止，人们对此还知之甚少。铁蛋白是许多生物中铁的主要存储和调节蛋白，它由一个蛋白质环和一个位于中心的亚铁核心组成。这项工作揭示了氧化态+ IV的早期act系元素（Th，Pu）与铁蛋白的相互作用以及与铁相比在生理pH下存储这些元素的能力。铁蛋白-or的负荷曲线表明Th ^IV就像铁在蛋白环上一样，使蛋白饱和（每个铁蛋白2840个Th原子）。互补光谱技术（分光光度法，红外光谱和X射线吸收光谱）与分子动力学相结合，提供了Th ^IV和Pu ^IV与铁蛋白相互作用的结构模型。光谱数据与MD计算的比较表明Th ^IV和Pu ^IV主要在蛋白质环上而不在亚铁核上复合。实际上，从XAS数据来看，没有证据表明Th和Pu环境中有Fe邻域。另一方面，来自蛋白质环氨基酸的羧酸盐和可能的其他碳酸根阴离子正在使阳离子配位球成形。从分子结构的观点来看，Th ^IV和Pu ^IV与铁蛋白（一种必需的铁存储蛋白）的相互作用是全面核毒理学的基石。

更新日期：2020-09-21

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