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

基本信息

项目摘要

Soluble guanylate cyclase (sGC) was isolated from bovine lung and its resonance Raman (RR) spectra were investigated for the reduced, CO-bound (CO-sGC), NO-bound (NO-sGC), oxidized, and oxidized NO-bound forms in the presence and absence of GTP.The RR spectra of sGC and CO-sGC,including the Fe-His stretch at 204 cm^<-1> and Fe-CO stretch at 473 cm^<-1>, were unaltered by binding of GTP,but apparent RR spectra of NO-sGC in the presence of GTP changed with time and concentrations of GTP.In the absence of GTP,the RR bands of N-O stretch (nu_<NO>) and Fe-No stretch (nu_<Fe-NO>) were observed at 1679 and 521 cm^<-1>, respectively. In its presence, two types of RR spectra were obtained, but after all GTP was exhausted by the enzymatic reaction, the spectrum for the absence of GTP was restoed. In one type of RR spectra, which appeared prior to the other, no NO-isotope sensitive band was detected and is heme spectrum was of a five-coordinate ferric high-spin type. In the other type, two nu_<NO> bands were observed at 1700 and 1681 cm^<-1>, which exhibited ^<15>NO isotopic frequency shifts of 21 and 34 cm^<-1>, respectively. Structural implications of the two types of RR spectra arizing from reaction intermediates have been discussed.
从牛肺中提取了可溶性鸟苷环化酶(SGC),研究了在GTP存在和不存在的情况下,还原的、CO结合的(CO-sGC)、非结合的(NO-sGC)、氧化的和氧化的非结合形式的共振拉曼光谱。,但在GTP存在下,NO-sGC的表观RR谱随时间和浓度的变化而变化。在没有GTP的情况下,N-O伸展(nu&lt;NO&gt;)和Fe-非伸展(nu&lt;Fe-NO&gt;)的RR谱带分别出现在1679和521 cm^&lt;-1&gt;在其存在下,可获得两种类型的RR光谱,但在酶反应耗尽所有GTP后,恢复了不含GTP的光谱。在一种类型的RR谱中,没有检测到非同位素敏感带,并且在另一种类型的RR谱中,它是一个五配位铁的高自旋型光谱。在另一种类型中,在1700和1681 cm;-1&gt;处观察到两条nu&lt;no&gt;带,它们分别表现出21和34 cm^&lt;-1&gt;无同位素频移。讨论了反应中间体产生的两种RR谱的结构含义。

项目成果

期刊论文数量(6)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
P.Jewsbury: "The distal-CO interaction in carbonmonoxy myoglobins : the molecular dynamics of 3 destal mutants." Biophys.J.68. 1283-1294 (1995)
P.Jewsbury:“碳单氧肌红蛋白中的远端 CO 相互作用:3 个远端突变体的分子动力学。”
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T.Kohzuma: "Spectroscopic and electrochemical studies on active-site transitions of the type 1 copper protein pseudoazurin from Achromobacter cycloclastes." J.Biol.Cham.270. 25733-25738 (1995)
T.Kohzuma:“来自环碎无色杆菌的 1 型铜蛋白假天青蛋白活性位点转变的光谱和电化学研究。”
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S.Hirota: "Observation of nonfundamental Fe-O_2 and Fe-CO vibrations and potential anharmonicities for oxy-and carbonmonoxy-hemoglobin ; Evidence supporting a new assignment of the Fe-C-O bending fundamental." J.Am.Chem.Soc.117. 821-822 (1995)
S.Hirota:“观察非基本 Fe-O_2 和 Fe-CO 振动以及氧和碳单氧血红蛋白的潜在非谐性;支持 Fe-C-O 弯曲基本原理新分配的证据。”
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D.A.Proshlyakov: "Microcirculating system for simultaneous determination of Raman and absorption spectra of enzymatic reaction intermediates and its application to the reaction of cytochrome c oxidase with hydrogen peroxide." Biochemistry. 35. 76-82 (1996
D.A.Proshlyakov:“同时测定酶反应中间体拉曼光谱和吸收光谱的微循环系统及其在细胞色素 C 氧化酶与过氧化氢反应中的应用。”
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M.Nagai: "Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan b37 mutant." J.Biol.Chem.270. 1636-1642 (1995)
M.Nagai:“使用色氨酸 b37 突变体对血红蛋白四级结构进行紫外共振拉曼研究。”
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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:
    $ 5.06万
  • 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:
    $ 5.06万
  • 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:
    $ 5.06万
  • 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:
    $ 5.06万
  • 项目类别:
    Grant-in-Aid for Specially Promoted Research
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
  • 批准号:
    12045264
  • 财政年份:
    2000
  • 资助金额:
    $ 5.06万
  • 项目类别:
    Grant-in-Aid for Scientific Research on Priority Areas
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:
    $ 5.06万
  • 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:
    $ 5.06万
  • 项目类别:
    Grant-in-Aid for Scientific Research on Priority Areas
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:
    $ 5.06万
  • 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:
    $ 5.06万
  • 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:
    $ 5.06万
  • 项目类别:
    Grant-in-Aid for Co-operative Research (A)

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靶向可溶性鸟苷酸环化酶作为治疗和预防心律失常的新策略:功效和机制
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    10604822
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    10845936
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    2023
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    10217246
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可溶性鸟苷酸环化酶的激活机制
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    10078617
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恢复鸟苷酸环化酶 C 信号传导以预防结直肠癌
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