...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Zn2+-Binding to the Voltage-Gated Proton Channel Hv1/VSOP
【24h】

Zn2+-Binding to the Voltage-Gated Proton Channel Hv1/VSOP

机译：Zn2 + - 绕电压门控质子通道HV1 / VSOP

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The voltage-gated proton channel (Hv1/VSOP) is inhibited by Zn2+, of which the binding site is located in the extracellular region. We utilized attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy to examine the coordination structure by monitoring protein structural changes induced by Zn2+-binding. The Zn2+-induced difference ATR-FTIR spectra of Hv1 showed IR features that can be assigned to the histidine C5-N1 and carboxylate-COO- stretches as well as amide I changes likely in alpha-helical peptide bonds. Analysis of vibrational frequencies indicated that the Zn2+ is coordinated by the anionic carboxylate with monodentate mode and by the histidine at N1 (N tau) position of the neutral imidazole form. Combined with quantum chemical calculations, the most probable coordination structure was proposed as a tetrahedral geometry with ligands of carboxylate and imidazole groups in addition to a water molecule.
机译：通过Zn2 +抑制电压门控质子通道（HV1 / VSOP），其中结合位点位于细胞外区域中。 我们利用衰减的总反射傅里叶变换红外（ATR-FTIR）光谱，通过监测Zn2 + - 桥接诱导的蛋白质结构变化来检查协调结构。 HV1的Zn2 +诱导差异ATR-FTIR光谱显示IR特征，其可以分配给组氨酸C5-N1和羧酸盐 - 共脉冲以及酰胺，Iα-螺旋肽键的变化。 振动频率的分析表明，Zn2 +由具有单常型模式的阴离子羧酸盐和中性咪唑形式的N1（n Tau）位置的组氨酸配位。 结合量子化学计算，除了水分子之外，还提出了最可能的配体，作为羧酸盐和咪唑基的配体的四面体几何形状。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号