铜转运蛋白C端金属结合域与Ag<sup>+</sup>及Hg<sup>2+</sup>的相互作用

引用本文: 朱云城, 王二琼, 马国林, 康彦彪, 赵林泓, 刘扬中. 铜转运蛋白C端金属结合域与Ag⁺及Hg²⁺的相互作用[J]. 物理化学学报, 2014, 30(1): 1-7. doi: 10.3866/PKU.WHXB201311263 shu

Citation: ZHU Yun-Cheng, WANG Er-Qiong, MA Guo-Lin, KANG Yan-Biao, ZHAO Lin-Hong, LIU Yang-Zhong. Interaction of C-Terminal Metal-Binding Domain of Copper Transport Protein with Ag⁺ and Hg²⁺[J]. Acta Physico-Chimica Sinica, 2014, 30(1): 1-7. doi: 10.3866/PKU.WHXB201311263 shu

铜转运蛋白C端金属结合域与Ag⁺及Hg²⁺的相互作用

基金项目:
国家自然科学基金(U1332210，21171156) (U1332210，21171156)

博士后基金(2013M541831)资助项目 (2013M541831)

摘要:

铜转运蛋白(CTR1)不仅参与铜的细胞摄取，而且在其它重金属离子的摄取过程中也发挥重要作用. 本文采用紫外-可见(UV-Vis)光谱，核磁共振(NMR)和质谱(MS)的方法，研究了人源CTR1 (hCTR1)的C端金属结合域(C8)与Ag⁺和Hg²⁺的相互作用. 研究表明，Ag⁺和Hg²⁺都能与C8结合，但二者与C8的结合机制明显不同. 每个C8分子可以结合两个Ag⁺离子，但一个Hg²⁺却可以与两个C8形成桥联. 此外，Ag⁺离子与C8的配位是一个中等速度的交换过程，而Hg²⁺离子则为快速交换过程. C8的半胱氨酸残基是两种离子的重要结合位点，同时组氨酸残基也参与两种金属离子的配位，其中Ag⁺优先结合组氨酸，而Hg²⁺则对半胱氨酸的结合具有显著的优势. 虽然HCH基序对C8 与金属配位至关重要，一些远端的其它氨基酸也可以参与C8 与银离子的配位，这可能与CTR1 在摄取Ag⁺过程中的金属转移机制相关. 这些结果为理解hCTR1 蛋白摄取重金属离子的作用机制提供了必要的信息.

关键词:

English

Interaction of C-Terminal Metal-Binding Domain of Copper Transport Protein with Ag⁺ and Hg²⁺

1.
Collaborative Innovation Center of Suzhou Nano Science and Technology, School of Chemistry and Materials Science, University of Science and Technology of China, Hefei 230026, P. R. China
Received Date: 04 November 2013
Available Online: 01 January 2014
Fund Project:
国家自然科学基金(U1332210，21171156)

博士后基金(2013M541831)资助项目

Abstract:

Copper transport protein (CTR1), which is essential for copper uptake, also plays an important role in the cellular uptake of other heavy metal ions. In this work, the interactions of the C-terminal metalbinding domain of human CTR1 (C8) with both Ag⁺ and Hg²⁺ were studied, using ultraviolet-visible (UV-Vis) spectroscopy, nuclear magnetic resonance (NMR) spectroscopy, and mass spectrometry (MS). The results showed that Ag⁺ and Hg²⁺ bind to C8 by different binding modes. Each C8 binds to two Ag⁺, whereas one Hg²⁺ crosslinks two C8 units. In addition, the coordination of Ag⁺ to C8 has an intermediate exchange rate, whereas the binding of Hg²⁺ to C8 has a fast exchange rate. The cysteine residue of C8 is one of the most important binding sites for both Ag⁺ and Hg²⁺. However, histidine residues are also involved in the metalbinding process. Ag⁺ binds histidine preferentially, whereas Hg²⁺ prefers to bind to cysteine residues. Although the HCH motif of C8 is crucial for metal binding, some other residues can also participate in the binding of Ag⁺. These residues may be involved in the metal-transfer process in the cellular uptake of Ag⁺ by CTR1. These results provide important information for a better understanding of the mechanism of cellular uptake of metal ions by CTR1.

Key words:

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1.
沈阳化工大学材料科学与工程学院沈阳 110142

铜转运蛋白C端金属结合域与Ag⁺及Hg²⁺的相互作用

English

Interaction of C-Terminal Metal-Binding Domain of Copper Transport Protein with Ag⁺ and Hg²⁺

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通讯作者: 陈斌, bchen63@163.com

中国化学会秘书处

铜转运蛋白C端金属结合域与Ag+及Hg2+的相互作用

English

Interaction of C-Terminal Metal-Binding Domain of Copper Transport Protein with Ag+ and Hg2+

CCS Chemistry：嵌段共聚物自组装成 “三明治”二维有机材料，实现纳米级压力传感功能

CCS Chemistry：颜徐州、鲍哲南： 你的皮肤可能是一片SPMs

CCS Chemistry：工作高效不疲劳，只须让催化剂动起来

CCS Chemistry：静电组装导向聚合- 聚电解质纳米凝胶量化制备新策略

CCS Chemistry：金黄色葡萄球菌醛基脱氢酶是如何识别特异性底物的？

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通讯作者: 陈斌, bchen63@163.com

中国化学会秘书处

铜转运蛋白C端金属结合域与Ag⁺及Hg²⁺的相互作用

Interaction of C-Terminal Metal-Binding Domain of Copper Transport Protein with Ag⁺ and Hg²⁺

CCS Chemistry：颜徐州、鲍哲南：你的皮肤可能是一片SPMs