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首页> 外文期刊>Biochemistry >Metal Selectivity of the Escherichia coli Nickel Metallochaperone, SlyD
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Metal Selectivity of the Escherichia coli Nickel Metallochaperone, SlyD

机译：大肠杆菌镍金属伴侣蛋白（SlyD）的金属选择性

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摘要

SlyD is a Ni(Ⅱ)-binding protein that contributes to nickel homeostasis in Escherichia coli. The C-terminal domain of SlyD contains a rich variety of metal-binding amino acids, suggesting broader metal binding capabilities, and previous work demonstrated that the protein can coordinate several types of first-row transition metals. However, the binding of SlyD to metals other than Ni(Ⅱ) has not been previously characterized. To improve our understanding of the in vitro metal-binding activity of SlyD and how it correlates with the in vivo function of this protein, the interactions between SlyD and the series of biologically relevant transition metals [Mn(Ⅱ), Fe(Ⅱ), Co(Ⅱ), Cu(I), and Zn(Ⅱ)] were examined by using a combination of optical spectroscopy and mass spectrometry. Binding of SlyD to Mn(Ⅱ) or Fe(Ⅱ) ions was not detected, but the protein coordinates multiple ions of Co(Ⅱ), Zn(Ⅱ), and Cu(I) with appreciable affinity (K_D values in or below the nanomolar range), highlighting the promiscuous nature of this protein. The order of affinities of SlyD for the metals examined is as follows: Mn(Ⅱ) and Fe(Ⅱ) < Co(Ⅱ) < Ni(Ⅱ)～ Zn(Ⅱ) 《 Cu(I). Although the purified protein is unable to overcome the large thermodynamic preference for Cu(I) and exclude Zn(Ⅱ) chelation in the presence of Ni(Ⅱ), in vivo studies reveal a Ni(Ⅱ)-specific function for the protein. Furthermore, these latter experiments support a specific role for SlyD as a [NiFe]-hydrogenase enzyme maturation factor. The implications of the divergence between the metal selectivity of SlyD in vitro and the specific activity in vivo are discussed.
机译：SlyD是一种Ni（Ⅱ）结合蛋白，有助于大肠杆菌中的镍稳态。 SlyD的C末端结构域包含多种与金属结合的氨基酸，表明具有更广泛的金属结合能力，并且先前的研究表明该蛋白质可以协调多种类型的第一行过渡金属。然而，SlyD与除Ni（Ⅱ）以外的金属的结合尚无定论。为了增进我们对SlyD的体外金属结合活性及其与该蛋白的体内功能的关系的了解，SlyD与一系列生物学相关的过渡金属[Mn（Ⅱ），Fe（Ⅱ）， Co（Ⅱ），Cu（I）和Zn（Ⅱ）]的使用是通过光谱学和质谱相结合来进行的。未检测到SlyD与Mn（Ⅱ）或Fe（Ⅱ）离子的结合，但该蛋白质以明显的亲和力协调Co（Ⅱ），Zn（Ⅱ）和Cu（I）的多个离子（K_D值在或低于纳摩尔范围），突出了这种蛋白质的混杂性质。 SlyD对金属的亲和力顺序为：Mn（Ⅱ）和Fe（Ⅱ）

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