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Elucidation of Dynamical Structures of Proteins by Ultraviolet Resonance Raman Spectroscopy

Elucidation of Dynamical Structures of Proteins by Ultraviolet Resonance Raman Spectroscopy
通过紫外共振拉曼光谱阐明蛋白质的动态结构
批准号:
63470141
负责人:
KITAGAWA Teizo
金额:
$4.42万
依托单位国家:
日本
项目类别:
Grant-in-Aid for General Scientific Research (B)
财政年份:
1988
资助国家:
日本
项目状态:
已结题
起止时间:
1988 至 1989

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中文摘要
翻译
蛋白质的动态结构对于理解蛋白质的结构-功能关系具有重要意义。由于振动光谱对分子的几何结构敏感,且响应时间足够快,我们采用紫外共振拉曼技术选择性地探测了芳香族残基的振动,其吸收带在200-240 nm附近。首先,确定了一个实验系统。将四次谐波引入1m氢拉曼移位器中,实现了对218 nm激光的隔离。用1.26米单色器上的太阳盲光倍增管测量拉曼散射。第二个顺序使用2400gr/mm的光栅。利用该系统,通过观察芳香族残基的共振增强拉曼光谱,研究了碳氧合血红蛋白(COHb)光解后四级结构的动力学特征。用秒…获得了波长为2 18 nm的10 ns激光脉冲,激发了拉曼散射当CO被氮气激光泵浦的染料激光器产生的419 nm处的10 ns脉冲或由其二次谐波的第一个H_2拉曼位移产生的436 nm的脉冲光解时,从光解脉冲到拉曼探测脉冲的延迟时间(DELTAt_D)在-100~500微秒之间变化。当DELTAt_d=-100mus和10 ns时,观察到的光谱彼此相同,与基于蛋白质结构7 ns变化的预期相反,但当DELTAt_d从10变化到20mus时,光谱模式发生了变化;1613和1011 cm^<-1>的谱带强度降低,878 cm^<-1>的谱带移动到883 cm^<-1>这些光谱变化表现为时间的光滑单调函数,表明在Delta_d=10mus附近没有中间体。在metHbF中加入效应剂(六磷酸肌醇)后,也观察到类似的光谱变化。因此,观察到的紫外共振拉曼光谱的变化归因于四元结构的变化,可能是由于α1-β2亚基界面上的β37-Trp和α42-Tyr的状态变化。较少
英文摘要
Dynamical structures of proteins is substantial to understand a structure-function relationship of proteins. Since vibrational spectroscopy is sensitive to a geometrical structure of molecules and its time response is sufficiently fast, we adopted ultraviolet resonance Raman technique to probe selectively the vibrations of aromatic residues with absorption bands around 200-240 nm. First, an experimental system was settled. The fourth harmonic of Nd:YAG laser was brought into a 1 m hydrogen Raman shifter, and the 218 nm radiation was isolated. Raman scattering was detected with a solar blind photomultiplier attached to a 1.26 m single monochomator. A grating with 2400 gr/mm was used in the second order. With this system dynamical features of quaternary structure of carbonmonoxy hemoglobin (COHb) after photolysis were pursued by observing resonance-enhanced Raman bands of the aromatic residues. The Raman scattering was excited by 10 ns pulses at 218 nm, which were obtained from the secon … More d H_2 Raman shift of the fourth harmonic of a Nd:YAG laser, while CO was photodissociated by 10-ns pulses at 419 nm generated by a nitrogen-laser pumped dye laser or by pulses at 436 nm generated from the first H_2 Raman shift of the second harmonic of the Nd:YAG laser The delay time (DELTAt_d) from the photolysis pulse to the Raman probe pulse was varied from -100 to 500 mus. The observed spectra obtained for DELTAt_d =-100 mus and 10 ns were the same as each other and as that obtained without the pump beam, contrary to expectations based on the reported 7-ns change of the protein structure, but the spectral pattern did change when DELTAt_d changed from 10 to 20 mus; the bands at 1613 and 1011 cm^<-1> decreased in intensity, and the band at 878 cm^<-1> shifted to 883 cm^<-1>. These spectral changes appeared as a smooth monotonous function of time, suggesting the absence of an intermediate around DELTA_d = 10 mus. A similar spectral change was also observed upon addition of an effector (inositol hexaphosphate) to metHbF. Accordingly, the observed changes of the UV resonance Raman spectra were attributed to a quaternary structure change, presumably to a status change of beta37-Trp and alpha42-Tyr at the alpha1-beta2 subunit interface. Less
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T.Ogura,S.Yoshikawa,T.Kitagawa: "Raman/Absorption Simultaneous Measurements for Cytochrome Oxidase Compound A at Room Temperature with a Novel Flow Apparatus." Biochemistry. 28. 8022-8027 (1989)
T.Ogura、S.Yoshikawa、T.Kitakawa:“使用新型流动装置在室温下同时测量细胞色素氧化酶化合物 A 的拉曼/吸收”。
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S.Hashimoto,T.Kotani,R.Nakajima,S.Ohtaki,I.Yamazaki,T.Kitagawa: "Resonance Raman characterization of hog thyroid peroxidase:A SERRS study." FEBS Letters. 248. 205-209 (1989)
S.Hashimoto、T.Kotani、R.Nakajima、S.Ohtaki、I.Yamazaki、T.Kitakawa:“猪甲状腺过氧化物酶的共振拉曼表征:SERRS 研究。”
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北川禎三(他): "新生化学実験講座" 東京化学同人, (1990)
北川帝三(等):《新化学实验教程》东京化学同人,(1990)
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21
    UV resonance Raman investigation on detection of higher order structural changes of heme proteins and elucidation of functional regulation mechanism
    • 批准号:
      24350086
    • 项目类别:
      Grant-in-Aid for Scientific Research (B)
    • 资助金额:
      $11.73万
    • 财政年份:
      2012
    • 负责人:
      KITAGAWA Teizo
    • 依托单位:
    Structural Chemistry on Information Transduction through Allosteric Effects in Heme Proteins
    • 批准号:
      21350098
    • 项目类别:
      Grant-in-Aid for Scientific Research (B)
    • 资助金额:
      $12.15万
    • 财政年份:
      2009
    • 负责人:
      KITAGAWA Teizo
    • 依托单位:
    Structural Chemistry Involved in Discrimination of Diatomic Ligands and Transduction Mechanism of Sensed Information of Gas Sensing Heme Proteins
    海外基金