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Resolution of a paradox by native mass spectrometry: facile occupation of all four metal binding sites in the dimeric zinc sensor SmtB

机译:通过天然质谱解决矛盾:在二聚体锌传感器SmtB中轻松占领所有四个金属结合位点

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摘要

The predominant species of the cyanobacterial metalloregulatory protein SmtB as observed by ESI-MS is a dimer with all four zinc binding sites occupied. Cellular biochemistry relies heavily upon the presence of a range of metal ions, including iron, zinc and copper. Although they are vital once bound to proteins, providing either structural or functional roles, the concentration of free ions has to be tightly regulated by homeostatic systems due to their inherent toxicity at high concentrations.
机译:ESI-MS观察到的主要蓝藻金属调节蛋白SmtB是一个二聚体,所有四个锌结合位点均被占据。细胞生物化学严重依赖于多种金属离子的存在,包括铁,锌和铜。尽管它们一旦与蛋白质结合就发挥了至关重要的作用,提供结构或功能上的作用,但由于其在高浓度下的固有毒性,游离离子的浓度必须由体内平衡系统严格控制。

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  • 来源
    《Chemical Communications》 |2013年第8期|813-815|共3页
  • 作者单位

    School of Life Sciences, The University of Warwick, Coventry, UK Department of Chemistry, The University of Warwick, Coventry, UK;

    Department of Chemistry, The University of Warwick, Coventry, UK;

    School of Life Sciences, The University of Warwick, Coventry, UK;

    School of Life Sciences, The University of Warwick, Coventry, UK;

    Department of Chemistry, The University of Warwick, Coventry, UK;

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  • 入库时间 2022-08-17 13:17:52

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