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本文引用的文献

1
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy.原子分辨率晶体学和X射线吸收光谱揭示的大肠杆菌CusF不寻常的铜（I）/银（I）配位
Protein Sci. 2007 Oct;16(10):2287-93. doi: 10.1110/ps.073021307.
2
Periplasmic metal-resistance protein CusF exhibits high affinity and specificity for both CuI and AgI.周质金属抗性蛋白CusF对CuI和AgI均表现出高亲和力和特异性。
Biochemistry. 2006 Sep 19;45(37):11096-102. doi: 10.1021/bi0612622.
3
Intermolecular transfer of copper ions from the CopC protein of Pseudomonas syringae. Crystal structures of fully loaded Cu(I)Cu(II) forms.丁香假单胞菌CopC蛋白中铜离子的分子间转移。完全负载的Cu(I)Cu(II)形式的晶体结构。
J Am Chem Soc. 2006 May 3;128(17):5834-50. doi: 10.1021/ja058528x.
4
A novel copper-binding fold for the periplasmic copper resistance protein CusF.周质铜抗性蛋白CusF的一种新型铜结合折叠结构。
Biochemistry. 2005 Aug 9;44(31):10533-40. doi: 10.1021/bi050827b.
5
A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.一种可能参与细菌细胞色素c氧化酶CuA中心组装的铜（I）蛋白。
Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3994-9. doi: 10.1073/pnas.0406150102. Epub 2005 Mar 7.
6
Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli.大肠杆菌铜转运外排系统CusCFBA的分子分析。
J Bacteriol. 2003 Jul;185(13):3804-12. doi: 10.1128/JB.185.13.3804-3812.2003.
7
Transition metal speciation in the cell: insights from the chemistry of metal ion receptors.细胞中的过渡金属形态：来自金属离子受体化学的见解
Science. 2003 May 9;300(5621):931-6. doi: 10.1126/science.1085049.
8
A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.CopC中的氧化还原开关：一种有趣的铜转运蛋白，可在不同位点结合一价铜和二价铜。
Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3814-9. doi: 10.1073/pnas.0636904100. Epub 2003 Mar 21.
9
The PcoC copper resistance protein coordinates Cu(I) via novel S-methionine interactions.PcoC铜抗性蛋白通过新型S-甲硫氨酸相互作用来配位Cu(I)。
J Am Chem Soc. 2003 Jan 15;125(2):342-3. doi: 10.1021/ja028935y.
10
The Cationminus signpi Interaction.阳离子减号π相互作用。
Chem Rev. 1997 Aug 5;97(5):1303-1324. doi: 10.1021/cr9603744.

通过CusF中阳离子-π相互作用和甲硫氨酸相互作用实现的Cu(I)识别

Cu(I) recognition via cation-pi and methionine interactions in CusF.

作者信息

Xue Yi, Davis Anna V, Balakrishnan Gurusamy, Stasser Jay P, Staehlin Benjamin M, Focia Pamela, Spiro Thomas G, Penner-Hahn James E, O'Halloran Thomas V

机构信息

Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.

出版信息

Nat Chem Biol. 2008 Feb;4(2):107-9. doi: 10.1038/nchembio.2007.57. Epub 2007 Dec 23.

DOI:10.1038/nchembio.2007.57
PMID:18157124
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2850561/
Abstract

Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.

摘要

富含甲硫氨酸的基序在包括CusF蛋白在内的铜转运因子中发挥着重要作用。在此我们表明，CusF利用了一个新的金属识别位点，其中Cu(I)从一个Met2His配体平面沿四方方向朝着一个保守的色氨酸位移。光谱研究表明，硫醚配位以及与色氨酸的强阳离子-π相互作用均能稳定金属结合。这种新型活性位点化学为控制偶然金属的氧化还原和取代化学提供了机制。