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首页> 外文期刊>Chemistry: A European journal >Elucidation of Metal-Ion Accumulation Induced by Hydrogen Bonds on Protein Surfaces by Using Porous Lysozyme Crystals Containing Rh-III Ions as the Model Surfaces
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Elucidation of Metal-Ion Accumulation Induced by Hydrogen Bonds on Protein Surfaces by Using Porous Lysozyme Crystals Containing Rh-III Ions as the Model Surfaces

机译：以含Rh-III离子的多孔溶菌酶晶体为模型表面，阐明蛋白质表面氢键引起的金属离子积累

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Metal-ion accumulation on protein surfaces is a crucial step in the initiation of small-metal clusters and the formation of inorganic materials in nature. This event is expected to control the nucleation, growth, and position of the materials. There remain many unknowns, as to how proteins affect the initial process at the atomic level, although multistep assembly processes of the materials formation by both native and model systems have been clarified at the macroscopic level. Herein the cooperative effects of amino acids and hydrogen bonds promoting metal accumulation reactions are clarified by using porous hen egg white lysozyme (HEWL) crystals containing Rh-III ions, as model protein surfaces for the reactions. The experimental results reveal noteworthy implications for initiation of metal accumulation, which involve highly cooperative dynamics of amino acids and hydrogen bonds: i) Disruption of hydrogen bonds can induce conformational changes of amino-acid residues to capture Rh-III ions. ii) Water molecules pre-organized by hydrogen bonds can stabilize Rh-III coordination as aqua ligands. iii) Water molecules participating in hydrogen bonds with amino-acid residues can be replaced by Rh-III ions to form polynuclear structures with the residues. iv) Rh-III aqua complexes are retained oil amino-acid residues through stabilizing hydrogen bonds even at low pH (approximate to 2). These metal-protein interactions including hydrogen bonds may promote native metal accumulation reactions and also may be useful in the preparation of new inorganic materials that incorporate proteins.
机译：蛋白质表面上的金属离子积累是引发小金属簇和自然界中无机材料形成的关键步骤。预计该事件将控制材料的成核，生长和位置。关于蛋白质如何影响原子级的初始过程，仍然存在许多未知数，尽管在宏观一级已经阐明了天然和模型系统形成材料的多步组装过程。在本文中，通过使用含有Rh-III离子的多孔鸡蛋清溶菌酶（HEWL）晶体作为反应的模型蛋白质表面，阐明了氨基酸和氢键促进金属积累反应的协同作用。实验结果揭示了引发金属积累的重要意义，其中涉及氨基酸和氢键的高度协同动力学：i）氢键的破坏可诱导氨基酸残基的构象变化以捕获Rh-III离子。 ii）通过氢键预组织的水分子可以稳定Rh-III作为水配体的配位。 iii）与氨基酸残基参与氢键的水分子可以被Rh-III离子取代，从而与残基形成多核结构。 iv）即使在低pH值（约2）下，Rh-III水络合物也可通过稳定氢键保留油氨基酸残基。这些包括氢键的金属-蛋白质相互作用可能会促进天然金属的积累反应，也可能用于制备结合蛋白质的新型无机材料。

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