Chemical foundation of the attenuation of methylmercury(II) cytotoxicity by metallothioneins.

Angels Leiva-Presa, Mercè Capdevila, Neus Cols, Silvia Atrian, Pilar González-Duarte
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引用次数: 15

Abstract

To elucidate the chemical interactions underlying the role of metallothioneins (MTs) in reducing the cytotoxicity caused by MeHg(II), we monitored in parallel by electronic absorption and CD spectroscopies the stepwise addition of MeHgCl stock solution to mammalian Zn(7)-MT1 and the isolated Zn(4)-alphaMT1 and Zn(3)-betaMT1 fragments. The incorporation of MeHg(+) into Zn(7)-MT and Zn(3)-betaMT entails total displacement of Zn(II) and unfolding of the protein. However, both features are only partial for Zn(4)-alphaMT. The different behavior observed for this fragment, whether isolated or constituting one of the two domains of Zn(7)-MT, indicates interdomain interactions in the whole protein. Overall, the binding properties of Zn(7)-MT, Zn(4)-alphaMT and Zn(3)-betaMT toward MeHg(+) are unprecedented. In addition, the sequestration of MeHg(+) by Zn(7)-MT and the concomitant release of Zn(II) are probably two of the main contributions in the detoxifying role of mammalian MT.

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甲基汞衰减的化学基础(II)金属硫蛋白的细胞毒性。
为了阐明金属硫蛋白(MTs)在降低甲基汞(II)引起的细胞毒性中的化学相互作用,我们通过电子吸收和CD光谱平行监测了将金属硫蛋白(MTs)原液逐步加入哺乳动物Zn(7)-MT1和分离的Zn(4)- α hamt1和Zn(3)- β amt1片段中。MeHg(+)结合到Zn(7)-MT和Zn(3)-betaMT中,导致Zn(II)的完全位移和蛋白质的展开。然而,这两个特征对Zn(4)- α - hamt来说只是部分的。该片段的不同行为,无论是被分离还是构成Zn(7)-MT的两个结构域之一,都表明整个蛋白质的结构域间相互作用。总之,Zn(7)-MT、Zn(4)- α - hamt和Zn(3)- β - amt对MeHg(+)的结合性能是前所未有的。此外,Zn(7)-MT对甲基汞(+)的固溶和Zn(II)的释放可能是哺乳动物MT解毒作用的两个主要原因。
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