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利用 MALDI-TOF-MS 和 XAS 分析金属硫蛋白与汞和/或硒形成的复合物。

MALDI-TOF-MS and XAS analysis of complexes formed by metallothionein with mercury and/or selenium.

机构信息

CAS-HKU Joint Laboratory of Metallomics on Health and Environment, & CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, & Beijing Metallomics Facility, & National Consortium for Excellence in Metallomics, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing, 100049, China.

University of Chinese Academy of Sciences, Beijing, 100049, China.

出版信息

Biometals. 2021 Dec;34(6):1353-1363. doi: 10.1007/s10534-021-00346-5. Epub 2021 Oct 2.

DOI:10.1007/s10534-021-00346-5
PMID:34599705
Abstract

Mercury (Hg) is highly toxic while selenium (Se) has been found to antagonize Hg. Both Hg and Se have been found to induce metallothioneins (MTs). In this study, the complexes formed by metallothionein-1 (MT-1) with HgCl and/or NaSeO was studied using matrix-assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF-MS) and X-ray absorption spectrometry (XAS). MALDI-TOF-MS and XAS indicated the formation of Hg-S bond or Se-S bond when MT-1 reacted with HgCl or NaSeO, respectively. The bond lengths of Hg-S and coordination number in MT-Hg are 2.41 ± 0.02 Å and 3.10 and in MT-Se are 2.50 ± 0.03 Å and 2.69. A MT-Se-Hg complex was formed when MT-1 reacted with both HgCl and NaSeO, in which the neighboring atom of Hg is Se, while the neighboring atoms of Se are S and Hg. Our study is an important step towards a better understanding of the interaction of HgCl and/or NaSeO with proteins like MT-1.

摘要

汞(Hg)是剧毒物质,而硒(Se)被发现可以拮抗汞。Hg 和 Se 都可以诱导金属硫蛋白(MTs)的产生。在这项研究中,采用基质辅助激光解吸/电离飞行时间质谱(MALDI-TOF-MS)和 X 射线吸收光谱(XAS)研究了金属硫蛋白-1(MT-1)与 HgCl 和/或 NaSeO 形成的配合物。MALDI-TOF-MS 和 XAS 表明,MT-1 分别与 HgCl 或 NaSeO 反应时形成 Hg-S 键或 Se-S 键。MT-Hg 中 Hg-S 键的键长和配位数分别为 2.41±0.02 Å 和 3.10,MT-Se 中 Hg-S 键的键长和配位数分别为 2.50±0.03 Å 和 2.69。当 MT-1 与 HgCl 和 NaSeO 反应时,形成了 MT-Se-Hg 配合物,其中 Hg 的相邻原子是 Se,而 Se 的相邻原子是 S 和 Hg。我们的研究是深入了解 HgCl 和/或 NaSeO 与 MT-1 等蛋白质相互作用的重要一步。

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