Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis

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• 作者：Yin Yang ; Feng Huang ; Thomas Huber ; Xun-Cheng Su
• 关键词：Protein labeling ; 8 ; Hydroxyquinoline ; Paramagnetic NMR spectroscopy ; Pseudocontact shift ; Paramagnetic relaxation enhancement
• 刊名：Journal of Biomolecular NMR
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：64
• 期：2
• 页码：103-113
• 全文大小：1,702 KB
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• 作者单位：Yin Yang (1)
  Feng Huang (1)
  Thomas Huber (2)
  Xun-Cheng Su (1)
  
  1. State Key Laboratory of Elemento-Organic Chemistry, Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Nankai University, Tianjin, 300071, China
  2. Research School of Chemistry, Australian National University, Canberra, ACT, 0200, Australia
  
• 刊物类别：Physics and Astronomy
• 刊物主题：Physics
  Biophysics and Biomedical Physics
  Polymer Sciences
  Biochemistry
  
• 出版者：Springer Netherlands
• ISSN：1573-5001

文摘

Design of a paramagnetic metal binding motif in a protein is a valuable way for understanding the function, dynamics and interactions of a protein by paramagnetic NMR spectroscopy. Several strategies have been proposed to site-specifically tag proteins with paramagnetic lanthanide ions. Here we report a simple approach of engineering a transition metal binding motif via site-specific labelling of a protein with 2-vinyl-8-hydroxyquinoline (2V-8HQ). The protein-2V-8HQ adduct forms a stable complex with transition metal ions, Mn(II), Co(II), Ni(II), Cu(II) and Zn(II). The paramagnetic effects generated by these transition metal ions were evaluated by NMR spectroscopy. We show that 2V-8HQ is a rigid and stable transition metal binding tag. The coordination of the metal ion can be assisted by protein sidechains. More importantly, tunable paramagnetic tensors are simply obtained in an α-helix that possesses solvent exposed residues in positions i and i + 3, where i is the residue to be mutated to cysteine, i + 3 is Gln or Glu or i − 4 is His. The coordination of a sidechain carboxylate/amide or imidazole to cobalt(II) results in different structural geometries, leading to different paramagnetic tensors as shown by experimental data. Keywords Protein labeling 8-Hydroxyquinoline Paramagnetic NMR spectroscopy Pseudocontact shift Paramagnetic relaxation enhancement