Higgins Khadine
Department of Chemistry, Salve Regina University, Newport, RI 02840, USA.
Inorganics (Basel). 2019 Aug;7(8). doi: 10.3390/inorganics7080104. Epub 2019 Aug 19.
Nickel is essential for the survival of many pathogenic bacteria. and require nickel for [NiFe]-hydrogenases. also requires nickel for urease. At high concentrations nickel can be toxic to the cell, therefore, nickel concentrations are tightly regulated. Metalloregulators help to maintain nickel concentration in the cell by regulating the expression of the genes associated with nickel import and export. Nickel import into the cell, delivery of nickel to target proteins, and export of nickel from the cell is a very intricate and well-choreographed process. The delivery of nickel to [NiFe]-hydrogenase and urease is complex and involves several chaperones and accessory proteins. A combination of biochemical, crystallographic, and spectroscopic techniques has been utilized to study the structures of these proteins, as well as protein-protein interactions resulting in an expansion of our knowledge regarding how these proteins sense and bind nickel. In this review, recent advances in the field will be discussed, focusing on the metal site structures of nickel bound to metalloregulators and chaperones.
镍对于许多致病细菌的生存至关重要。[NiFe]氢化酶需要镍。脲酶也需要镍。在高浓度时,镍对细胞可能有毒,因此,镍的浓度受到严格调控。金属调节蛋白通过调节与镍进出相关基因的表达来帮助维持细胞内的镍浓度。镍进入细胞、将镍递送至靶蛋白以及从细胞中输出镍是一个非常复杂且精心编排的过程。将镍递送至[NiFe]氢化酶和脲酶的过程很复杂,涉及多种伴侣蛋白和辅助蛋白。已经利用生物化学、晶体学和光谱学技术的组合来研究这些蛋白质的结构以及蛋白质 - 蛋白质相互作用,从而扩展了我们对这些蛋白质如何感知和结合镍的认识。在这篇综述中,将讨论该领域的最新进展,重点是与金属调节蛋白和伴侣蛋白结合的镍的金属位点结构。