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Use of XAS for the elucidation of metal structure and function: applications to nickel biochemistry molecular toxicology and carcinogenesis.

机译:XAS用于阐明金属结构和功能的用途:在镍生物化学分子毒理学和致癌作用中的应用。

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摘要

Nickel has been shown to be an essential trace element involved in the metabolism of several species of bacteria, archea, and plants. In these organisms, nickel is involved in enzymes that catalyze both non-redox (e.g., urease, glyoxalase I) and redox (e.g., hydrogenase, carbon monoxide dehydrogenase, superoxide dismutase) reactions, and proteins involved in the transport, storage, metallocenter assembly, and regulation of nickel concentration have evolved. Studies of structure/function relationships in nickel biochemistry reveal that cysteine ligands are used to stabilize the Ni(III/II) redox couple. Certain nickel compounds have also been shown to be potent human carcinogens. A likely target for carcinogenic nickel is nuclear histone proteins. Here we present X-ray absorption spectroscopic studies of a model Ni peptide designed to help characterize the structure of the nickel complexes formed with histones and place them in the context of nickel structure/function relationships, to gain insights into the molecular mechanism of nickel carcinogenesis.
机译:镍已被证明是参与多种细菌,古细菌和植物代谢的必需微量元素。在这些生物中,镍参与催化非氧化还原酶(例如脲酶,乙二醛酶I)和氧化还原酶(例如氢化酶,一氧化碳脱氢酶,超氧化物歧化酶)反应的酶,以及参与运输,储存和金属中心组装的蛋白质,并且镍浓度的调节已经发展。镍生物化学中结构/功能关系的研究表明,半胱氨酸配体用于稳定Ni(III / II)氧化还原对。某些镍化合物也已被证明是有效的人类致癌物。致癌镍的可能靶标是核组蛋白。在这里,我们介绍了一种模型镍肽的X射线吸收光谱研究,该肽旨在帮助表征与组蛋白形成的镍配合物的结构,并将其置于镍结构/功能关系的背景下,以深入了解镍致癌的分子机理。 。

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