Understanding the role that metal ions play in biological and material processes is critical to addressing a number of diseases and problems facing society today. There have been a number of studies that have begun to approach this concern from a myriad of different perspectives. However, there is still a considerable lack of understanding concerning the mechanisms and structures of metal-related problems, specifically biological and medical-related issues. Understanding the mechanism of ingestion and uptake of metals into the human body is critical to addressing many diseases such as Alzheimer’s and certain types of cancers. Using computational techniques, this work adds to the overall understanding of metal interactions with proteins by focusing on metal ion interactions with the amino acid, histidine, one of the most common sites of metal attachment. In this work, the geometries of single and dual histidines attached to Ni²⁺, Cu²⁺, and Zn²⁺ ions at B3LYP/6-311G(d) are presented. The results show stable octahedral complexes associated with each of the metal ions. Free energy calculations suggest that all three complexes are spontaneous in the formation of the dual histidine-metal complexes. Nickel and copper are spontaneous in the formation of the single histidine complex, although the copper complex undergoes slight geometric changes. Zinc is found to be nonspontaneous in forming the single histidine complex. Finally, the reduction potential of the single histidine-metal complex is presented. All of the complexes show positive reduction potentials. However, the nickel and copper complexes undergo geometrical changes to adopt a square planar conformation.

The impact of metal ions in biological systems is of great importance to understanding a diverse number of diseases. By understanding the fundamentals of select ions complexed with histidines, greater understanding of the mechanisms of actions these ions play in health may be elucidated. This work presents initial structures and thermodynamics of histidine complexes with nickel, copper, and zinc metal ions.

中文翻译：

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DFT研究分离了六配位八面体络合物中组氨酸与金属离子（Ni2 +，Cu2 +，Zn2 +）的相互作用。

了解金属离子在生物和物质过程中的作用对于解决当今社会面临的许多疾病和问题至关重要。有许多研究已从无数不同的角度开始着手解决这一问题。但是，对于与金属有关的问题，特别是与生物和医学有关的问题的机理和结构，仍然缺乏足够的了解。了解金属摄入和摄取到人体中的机制对于解决许多疾病，例如老年痴呆症和某些类型的癌症至关重要。通过使用计算技术，这项工作将重点放在金属离子与氨基酸，组氨酸，金属附着的最常见位置之一。在这项工作中，与镍相连的单组氨酸和双组氨酸的几何形状^给出了B3LYP / 6-311G（d）处的2 ⁺，Cu ²⁺和Zn ²⁺离子。结果显示与每种金属离子缔合的稳定的八面体络合物。自由能的计算表明，所有三个络合物在组氨酸-金属双重络合物的形成中都是自发的。镍和铜是单组氨酸配合物的自发形成，尽管铜配合物会发生轻微的几何变化。发现锌在形成单个组氨酸复合物中是非自发的。最后，给出了单个组氨酸-金属配合物的还原电位。所有的配合物都显示出正的还原潜力。然而，镍和铜络合物经历几何变化以采用正方形平面构型。

金属离子对生物系统的影响对于了解多种疾病非常重要。通过了解与组氨酸络合的精选离子的基本原理，可以阐明对这些离子在健康中发挥作用的机制的更深入的了解。这项工作介绍了组氨酸与镍，铜和锌金属离子的配合物的初始结构和热力学。