Observation of the Imidazole-Imidazolium Hydrogen Bonds Responsible for Selective Proton Conductance in the Influenza A M2 Channel,Journal of the American Chemical Society

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Observation of the Imidazole-Imidazolium Hydrogen Bonds Responsible for Selective Proton Conductance in the Influenza A M2 Channel
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2020-01-23 , DOI: 10.1021/jacs.9b09985
Riqiang Fu ₁ , Yimin Miao ₂ , Huajun Qin ₂ , Timothy A Cross _{1,

2}

Affiliation

The integral membrane M2 protein is a 97-residue membrane protein that assembles as a tetramer to conduct protons at a slow rate (102-103/s) when activated by low pH. The proton conductance mechanism has been extensively debated in the literature, but it is accepted that the proton conductance is facilitated by hydrogen bonds involving the His37 residues. However, the hydrogen bonding partnership remains unresolved. Here, we report on the measurement of 15N-15N J-couplings of 15N His37-labeled full length M2 (M2FL) protein from Influenza A virus embedded in synthetic liquid crystalline lipid bilayers using two-dimensional J-resolved NMR spectroscopy. We experimentally observed the hydrogen-bond mediated J-couplings between Nδ1 and Nε2 of adjacent His37 imidazole rings, providing direct evidence for the existence of various imidazolium-imidazole hydrogen-bonding geometries in the histidine tetrad at low pH, thus validating the proton conduction mechanism in the M2FL protein by which the proton is transferred through the breaking and reforming of the hydrogen-bonds between pairs of His37 residues.

中文翻译：

对甲型流感 M2 通道中负责选择性质子传导的咪唑-咪唑鎓氢键的观察

完整的膜 M2 蛋白是一种含有 97 个残基的膜蛋白，当被低 pH 激活时，它会组装为四聚体，以缓慢的速率 (102-103/s) 传导质子。质子传导机制在文献中已被广泛讨论，但公认的是质子传导是由涉及 His37 残基的氢键促进的。然而，氢键伙伴关系仍未解决。在这里，我们报告了使用二维 J 分辨核磁共振光谱测量嵌入合成液晶脂双层中的甲型流感病毒的 15N His37 标记全长 M2 (M2FL) 蛋白的 15N-15N J 偶联。我们通过实验观察到相邻 His37 咪唑环的 Nδ1 和 Nε2 之间的氢键介导的 J 偶联，

更新日期：2020-01-23

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