Structure and Function Study of Light-Driven Ion Pumps

光驱动离子泵的结构与功能研究

基本信息

  • 批准号:
    09833002
  • 负责人:
  • 金额:
    $ 2.24万
  • 依托单位:
  • 依托单位国家:
    日本
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
  • 财政年份:
    1997
  • 资助国家:
    日本
  • 起止时间:
    1997 至 1998
  • 项目状态:
    已结题

项目摘要

This research project aims at revealing the correlation between structure and function of light-driven ion pumps that possess retinal molecule as the chromophore. The target molecules are bacteriorhodopsin (bR) as a light-driven proton pump, halorhodopsin (hR) as a light-driven chloride pump, and rhodopsin (Rh) as a light-sensor in our vision. Fourier-transform infrared (FTIR) spectroscopy of these proteins as well as their mutants and isotope-labeled molecules provided the following results.(1) Location and orientation of a water molecule present between the Schiff base and Asp85 of bR were studied by means of polarized FTIR spectroscopy, It was revealed that the water, which plays an important role in proton transfer, is bound to protein through hydrogen bonding.(2) Polarized FTIR spectroscopy of bR revealed the structural changes of protein side upon photoisomerization. Many structural features on hydrogen bonding network in bR are changed.(3) Water structural changes in the N intermediate of bR were measured for the wild-type and mutant proteins, and a functional water at the cytoplasmic region was found. In addition, specific protein structural changes were newly observed by polarized FTIR spectroscopy.(5) Time-resolved step-scan FTIR spectroscopy of bR mutants provided the structural information on the 0 intermediate, an intermediate appearing at the last stage of the photocycle of bR.(4) Two L intermediates of hR were revealed by low-temperature FTIR spectroscopy, which could be correlated with change in accessibility in chloride pumping.(5) Water molecules in Rh were discovered by low-temperature FTIR spectroscopy.
本研究旨在揭示以视网膜分子为生色团的光驱动离子泵的结构与功能之间的关系。目标分子是作为光驱动质子泵的细菌视紫红质(BR),作为光驱动氯化物泵的卤视紫红质(HR),以及作为我们视觉中的光传感器的视紫红质(Rh)。这些蛋白质及其突变体和同位素标记分子的傅里叶变换红外光谱研究结果如下:(1)利用偏振傅里叶变换红外光谱研究了BR的Schiff碱和Asp85之间的水分子的位置和取向,揭示了在质子转移中起重要作用的水通过氢键与蛋白质结合。(2)BR的偏振FTIR光谱揭示了蛋白质光异构化过程中蛋白质侧结构的变化。BR中氢键网络的许多结构特征都发生了变化。(3)测定了野生型和突变型BR中N中间体的水结构变化,并在细胞质区域发现了功能水。此外,偏振傅里叶变换红外光谱还观察到了特定蛋白质结构的变化。(5)BR突变体的时间分辨步进扫描FTIR光谱提供了0中间体的结构信息,该中间体出现在BR光周期的最后阶段。(4)低温傅立叶变换红外光谱揭示了HR的两个L中间体,这可能与氯泵中可及性的变化有关。(5)低温FTIR光谱发现了Rh中的水分子。

项目成果

期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
Nishimura, S., Kandori, H., and Maeda, A.: "Interaction between Photoactivated Rhodopsin and the C-Terminal Peptide of Transducin a Subunit Studied by FTIR Spectroscopy."Biochemistry. 37. 15816-15824 (1998)
Nishimura, S.、Kandori, H. 和 Maeda, A.:“通过 FTIR 光谱研究光激活视紫红质与转导蛋白亚基 C 端肽之间的相互作用。”生物化学。
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  • 影响因子:
    0
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  • 通讯作者:
Nishimura,S.: "Structural Dynamics of Water and the Peptide Backbone around the Schiff Base Associated with the Light-Activated Process of Octopus Rhodopsin" Biochemistry. 36. 864-870 (1997)
Nishimura,S.:“与章鱼视紫红质光激活过程相关的水和希夫碱周围肽主链的结构动力学”生物化学。
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    0
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Yamazaki, Y.: "Interaction of the Protonated Schiff Base with the Peptide Backbone of Valine 49 and the Intervening Water Molecule in the N Photointermediate of Bacteriorhodopsin" Biochemistry. 37. 1559-1564 (1998)
Yamazaki, Y.:“质子化席夫碱与缬氨酸 49 的肽主链以及细菌视紫红质 N 光中间体中的介入水分子的相互作用”生物化学。
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    0
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Nishimura,S.: "Transmembrane Signaling Mediated by Water in Bovine Rhodopsin" Photochem.Photobiol. 66. 796-801 (1997)
Nishimura,S.:“牛视紫红质中水介导的跨膜信号传导”Photochem.Photobiol。
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  • 影响因子:
    0
  • 作者:
  • 通讯作者:
Nagata, T., Terakita, A., Kandori, H., Shichida, Y., and Maeda, A.: "The Hydrogen Bonding Network of Water Molecules and the Peptide Backbone in the Region Connecting Asp83, Gly120 and Glu113 in Bovine Rhodopsin."Biochemistry. 37. 17216-17222 (1998)
Nagata, T.、Terakita, A.、Kandori, H.、Shichida, Y. 和 Maeda, A.:“牛视紫红质中连接 Asp83、Gly120 和 Glu113 的区域中水分子和肽主链的氢键网络
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    0
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KANDORI Hideki其他文献

KANDORI Hideki的其他文献

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{{ truncateString('KANDORI Hideki', 18)}}的其他基金

Structural analysis of primate blue-sensitive pigment by FTIR spectroscopy
FTIR 光谱法分析灵长类蓝敏色素的结构
  • 批准号:
    25620011
  • 财政年份:
    2013
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Challenging Exploratory Research
FTIR spectroscopy of non-photoreceptive membrane proteins
非感光膜蛋白的 FTIR 光谱
  • 批准号:
    22247024
  • 财政年份:
    2010
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Scientific Research (A)
Infrared Spectroscopy of Newly Discovered Archaeal-type Rhodopsins
新发现的古菌型视紫红质的红外光谱
  • 批准号:
    19370067
  • 财政年份:
    2007
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Molecular mechanism of light-sensor proteins containing a flavin
含黄素的光传感器蛋白的分子机制
  • 批准号:
    17370057
  • 财政年份:
    2005
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Where is the pump switch of bacteriorhodopsin located?
细菌视紫红质的泵开关位于哪里?
  • 批准号:
    14380316
  • 财政年份:
    2002
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
偏光赤外分光を用いたロドプシンの動的構造解析
使用偏振红外光谱分析视紫红质的动态结构
  • 批准号:
    11480193
  • 财政年份:
    1999
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B).
Reaction Dynamics in Manybody Chemical Systems : Specificity in Biomolecular Reactions
多体化学系统中的反应动力学:生物分子反应的特异性
  • 批准号:
    10206206
  • 财政年份:
    1998
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Scientific Research on Priority Areas (B)
Role of Water Molecules in Proton Transfer in Bacteriorhodopsin
水分子在细菌视紫红质质子转移中的作用
  • 批准号:
    07839003
  • 财政年份:
    1995
  • 资助金额:
    $ 2.24万
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
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