Time-Resolved Vibrational Spectroscopic Investigation of Ultrafast Protein Dynamics Coupled with Photoreaction

超快蛋白质动力学与光反应耦合的时间分辨振动光谱研究

基本信息

项目摘要

In many biological systems a localized small structural change extends spatially to mesoscopic dimensions to achieve a physiological function, and higher-order structural changes of proteins are essential to this process. Myoglobin (Mb) is one of the best molecules for studying such features of proteins, because photodissociation of CO from carbonmonoxyMb (MbCO), a localized reaction, takes place within 50 fs like a step-function with a quantum yield of nearly unity. It is know from x-ray studies that the iron atom moves out of the porphyrin plane by 〜0.3 A and the core-size expands by 0.05A upon deligation of CO. To explore the protein dynamics involved in this process, we have investigated picosecond time-resolved resonance Raman spectra of photodissociated MbCO.Close inspection of the spectra of deoxyMb following CO photolysis in the 1300-1650 cm^<-1> region revealed that the core-size expansion of porphyrin ring is completed within the instrumental response time (〜2 ps). In contrast, changes in the intensity and frequency of the Fe-His stretching mode (VFe-His) occurred in picoseconds, suggesting appreciable time evolution for the Fe displacement from the porphyrin plane. The same behaviors were observed for the model compound of the heme group without protein matrix. Therefore, this reflects an intrinsic property of heme itself. On the other hand, the frequency of the VFe-His mode changed with a time constant of 〜100 ps. This frequency change was not seen for the model compound without the protein matrix. Therefore, this must be caused by tertiary structural changes of the protein. Temporal changes of the anti-Stokes Raman intensity of the V_4 and V_7 bands demonstrated immediate generation of the vibrationally excited heme upon photolysis and subsequent decay of the vibrationally excited population with the time constants of 1.1±0.6 and 1.9±0.6 ps, respectively.
在许多生物系统中,局部的小结构变化在空间上延伸到介观维度以实现生理功能,并且蛋白质的高阶结构变化对该过程至关重要。肌红蛋白(Mb)是研究蛋白质这些特征的最佳分子之一,因为CO从一氧化碳Mb(Mb CO)的光解离是一个局部化反应,在50 fs内发生,像一个阶跃函数,量子产率几乎为1。从X射线研究中得知,铁原子移出卟啉平面约0.3埃,核心尺寸扩大了0.05埃,CO的deligation. To探讨蛋白质动力学参与这一过程中,我们已经研究了皮秒时间分辨共振拉曼光谱的光解MbCO。仔细检查的光谱脱氧Mb CO光解后,在1300-1650 cm ↑ [2]<-1>区域显示,核心尺寸扩大的卟啉环内完成的仪器响应时间(102 ps)。与此相反,Fe-His伸缩模式(VFe-His)的强度和频率的变化发生在皮秒,这表明从卟啉平面的Fe位移明显的时间演化。对于没有蛋白质基质的血红素组的模型化合物,观察到相同的行为。因此,这反映了血红素本身的内在属性。另一方面,VFe-His模的频率随着时间常数100 ps而变化。对于不含蛋白质基质的模型化合物,未观察到该频率变化。因此,这一定是由蛋白质的三级结构变化引起的。V_4和V_7带的反斯托克斯拉曼强度随时间的变化表明,振动激发态的血红素在光解后立即产生,随后振动激发态的布居数衰减,时间常数分别为1.1±0.6和1.9±0.6 ps。

项目成果

期刊论文数量(50)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
T.TOMITA: "Purification of Bovine Soluble Guanylate Cyclase and ADP-Ribosylation on Its Small Subunit by Bacterial Toxins"J.Biochem. 122. 531 (1997)
T.TOMITA:“通过细菌毒素纯化牛可溶性鸟苷酸环化酶及其小亚基上的 ADP-核糖基化”J.Biochem。
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N.Haruta, M.Aki, S.Ozaki, Y.Watanabe, T.Kitagawa: "Protein Conformation Change of Myoglobin upon Ligand Binding Probed by Ultraviolet Resonance Raman Spectroscopy"Biochemistry. 40. 6956-6963 (2001)
N.Haruta、M.Aki、S.Ozaki、Y.Watanabe、T.Kitakawa:“通过紫外共振拉曼光谱探测配体结合时肌红蛋白的蛋白质构象变化”生物化学。
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Y.MIZUTANI: "Ultrafast structural relaxation of myoglobin following photodissociation of carbon monoxide probed by time-resolved resonance Raman spectroscopy"J.Phys.Chem.. 105. 10992 (2001)
Y.MIZUTANI:“通过时间分辨共振拉曼光谱探测一氧化碳光解后肌红蛋白的超快结构弛豫”J.Phys.Chem.. 105. 10992 (2001)
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Y.MIZUTANI: "Ultrafast structural relaxation of myoglobin following photodissociation of carbon monoxide probed by time-resolved resonance Raman spectroscopy"J. Phys. Chem. 105. 10992 (2001)
Y.MIZUTANI:“通过时间分辨共振拉曼光谱探测一氧化碳光解后肌红蛋白的超快结构弛豫”J。
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M.Aki他5名: "Uv resonance Raman characterization of model compounds of Tyr244 of Bovine cytoclirome c oxidase in its neutral-, deprotonated anion-, and deprotonated neutral radical-forms ; Effects of covalent binding between tyrosine and histidine"Journal o
M.Aki 和其他 5 人:“牛细胞色素 c 氧化酶 Tyr244 模型化合物的紫外共振拉曼表征(中性、去质子化阴离子和去质子化中性自由基形式;酪氨酸和组氨酸之间共价结合的影响”)杂志
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KITAGAWA Teizo其他文献

KITAGAWA Teizo的其他文献

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{{ truncateString('KITAGAWA Teizo', 18)}}的其他基金

UV resonance Raman investigation on detection of higher order structural changes of heme proteins and elucidation of functional regulation mechanism
紫外共振拉曼研究检测血红素蛋白高阶结构变化并阐明功能调节机制
  • 批准号:
    24350086
  • 财政年份:
    2012
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Structural Chemistry on Information Transduction through Allosteric Effects in Heme Proteins
通过血红素蛋白变构效应进行信息转导的结构化学
  • 批准号:
    21350098
  • 财政年份:
    2009
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Structural Chemistry Involved in Discrimination of Diatomic Ligands and Transduction Mechanism of Sensed Information of Gas Sensing Heme Proteins
双原子配体识别的结构化学及气敏血红素蛋白传感信息的转导机制
  • 批准号:
    19350089
  • 财政年份:
    2007
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Development of Detection Methods of Dynamical Higher Order Structures of Proteins and Its Application to Elucidation of Structure-Function Relations of Proteins.
蛋白质动态高阶结构检测方法的发展及其在阐明蛋白质结构功能关系中的应用。
  • 批准号:
    14001004
  • 财政年份:
    2002
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Specially Promoted Research
Time-Resolved Vibrational Spectroscopic Study of Higher Order Structural Changes of Protein Induced by Nanosecond Temperature Jump.
纳秒温度跳跃引起的蛋白质高阶结构变化的时间分辨振动光谱研究。
  • 批准号:
    10480187
  • 财政年份:
    1998
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B).
Molecular Science on the Specific Roles of Metal Ions in Biological Functions.
金属离子在生物功能中特定作用的分子科学。
  • 批准号:
    08249105
  • 财政年份:
    1996
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Scientific Research on Priority Areas
Elucidation of Reaction Mechanisms of Biological Nitric Oxide by Vibrational Spectroscopy
振动光谱法阐明生物一氧化氮的反应机制
  • 批准号:
    07454157
  • 财政年份:
    1995
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Detection of Fast Conformation Changes of Proteins by Time-Resolved Resonance Raman Spectroscopy
通过时间分辨共振拉曼光谱检测蛋白质的快速构象变化
  • 批准号:
    05453212
  • 财政年份:
    1993
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for General Scientific Research (B)
Molecular Science for Elucidation of Proton Active Transport and Electron Transfers through Proteins.
通过蛋白质阐明质子主动传输和电子转移的分子科学。
  • 批准号:
    02453157
  • 财政年份:
    1990
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for General Scientific Research (B)
Quantum Theory and Spectroscopy of Proteins as Biomachines
作为生物机器的蛋白质的量子理论和光谱学
  • 批准号:
    02305013
  • 财政年份:
    1990
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Grant-in-Aid for Co-operative Research (A)

相似国自然基金

myoglobin基因在前庭毛细胞发育和功能中的作用及其分子机制研究
  • 批准号:
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Novel anti-fibrotic properties of heme binding proteins including Neuroglobin, Myoglobin, and Hemoglobin in comparison with Cytoglobin in vitro and in vivo
与细胞红蛋白相比,血红素结合蛋白(包括神经红蛋白、肌红蛋白和血红蛋白)在体外和体内的新型抗纤维化特性
  • 批准号:
    22K08083
  • 财政年份:
    2022
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    $ 9.09万
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Investigation for the molecular biological role of myoglobin in the cerebral aneurysm walls
脑动脉瘤壁中肌红蛋白分子生物学作用的研究
  • 批准号:
    22K09232
  • 财政年份:
    2022
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    $ 9.09万
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Modification of mitochondrial function by myoglobin located in inner-mitochondria space in myocytes
位于肌细胞线粒体内空间的肌红蛋白对线粒体功能的修饰
  • 批准号:
    21H03318
  • 财政年份:
    2021
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    $ 9.09万
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Function and biomedical implications of myoglobin in breast cancer
肌红蛋白在乳腺癌中的功能和生物医学意义
  • 批准号:
    396924190
  • 财政年份:
    2018
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    $ 9.09万
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    Research Grants
Tracking the structural dynamics of myoglobin and its heme structure by gas-phase resonance Raman spectroscopy combined with theory and computation determines
通过气相共振拉曼光谱结合理论和计算来跟踪肌红蛋白及其血红素结构的结构动力学确定
  • 批准号:
    17K18080
  • 财政年份:
    2017
  • 资助金额:
    $ 9.09万
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    Grant-in-Aid for Young Scientists (B)
Real-time myoglobin saturation measurement to assess benefit of RBC transfusion
实时肌红蛋白饱和度测量以评估红细胞输血的益处
  • 批准号:
    9181365
  • 财政年份:
    2015
  • 资助金额:
    $ 9.09万
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Real-time myoglobin saturation measurement to assess benefit of RBC transfusion
实时肌红蛋白饱和度测量以评估红细胞输血的益处
  • 批准号:
    8880786
  • 财政年份:
    2015
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    $ 9.09万
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Noninvasive compact device to monitor myoglobin saturation in anemia and critical illness
无创紧凑型设备,用于监测贫血和危重疾病中的肌红蛋白饱和度
  • 批准号:
    9974985
  • 财政年份:
    2015
  • 资助金额:
    $ 9.09万
  • 项目类别:
Real-time myoglobin saturation measurement to assess benefit of RBC transfusion
实时肌红蛋白饱和度测量以评估红细胞输血的益处
  • 批准号:
    9328144
  • 财政年份:
    2015
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    $ 9.09万
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Functional diversification of myoglobin in the lungfish
肺鱼肌红蛋白的功能多样化
  • 批准号:
    263938600
  • 财政年份:
    2015
  • 资助金额:
    $ 9.09万
  • 项目类别:
    Research Grants
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