鉄結合性タンパク質によるプルトニウムとトリウムの取り込み

鉄結合性タンパク質によるプルトニウムとトリウムの取り込み

WRHIからのお知らせおすすめ

ゼロカーボンエネルギー研究所 津島悟特任准教授の共著論文

“Interaction of Th(IV), Pu(IV) and Fe(III) with ferritin protein: how similar?”

が、Journal of Synchrotron Radiation  にオンライン掲載されました。
DOI: 10.1107/S1600577521012340

詳しくはこちら 

 

<Abstract>

Ferritin is the main protein of Fe storage in eukaryote and prokaryote cells. It is a large multifunctional, multi-subunit protein consisting of heavy H and light L subunits. In the field of nuclear toxicology, it has been suggested that some actinide elements, such as thorium and plutonium at oxidation state +IV, have a comparable `biochemistry’ to iron at oxidation state +III owing to their very high tendency for hydrolysis and somewhat comparable ionic radii. Therefore, the possible mechanisms of interaction of such actinide elements with the Fe storage protein is a fundamental question of bio-actinidic chemistry. We recently described the complexation of Pu(IV) and Th(IV) with horse spleen ferritin (composed mainly of L subunits). In this article, we bring another viewpoint to this question by further combining modeling with our previous EXAFS data for Pu(IV) and Th(IV). As a result, the interaction between the L subunits and both actinides appears to be non-specific but driven only by the density of the presence of Asp and Glu residues on the protein shell. The formation of an oxyhydroxide Th or Pu core has not been observed under the experimental conditions here, nor the interaction of Th or Pu with the ferric oxyhydroxide core.