Relationship between structural changes of protein and function of abnormal hemoglobin.

蛋白质结构变化与异常血红蛋白功能的关系。

• 批准号: 05670116
• 负责人: NAGAI Masako
• 金额: $ 1.34万
• 依托单位: Kanazawa University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (C)
• 财政年份: 1993
• 资助国家: 日本
• 起止时间: 1993 至 1994
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-05670116/
• 关键词: Hemoglobin; Ultraviolet Resonance Raman; Circular Dichroism; Protein Structure; Function of Hemoglobin; Aromatic Amino Acids; 赤外分光; 円二色性; 異常血色素; 共鳴ラマン

X-ray crystallographic studies have shown that the deoxy and liganded forms of hemoglobin (Hb) poseesee two distinct quaternary structures named T-and R-states, respectively. Cooperative oxygenation to Hb has been explained in terms of a reversible transition between the two quaternary structures upon partial ligation to the four hemes. Environmental changes of tyrosine (Tyr) and tryptophan (Trp) residues of Hb upon its T-to-R transition of quaternary structure was ivestigated with ultraviolet resonance Raman (UVRR) spectroscopy and circular dichroism (CD) . To characterize the spectral change of Trp beta37 at alpha_1beta_2 interface due to the quaternary structure transition, the UVRR spectra of Hb A were compared with the corresponding spectra of Hb Hirose in which Trp beta37 is replaced by serine (Ser) . Difference spectrum between deoxyHb A and deoxyHb Hirose gave rise to only Trp RR bands, which were reasonably ascribed to Trp beta37 in deoxyHb A.Comparison of the Hb A-Hb Hirose difference spectra in the oxy and deoxy states revealed that the oxygenation-induced changes of Trp RR bands arose mostly from Trp beta37 and the remaining minor part from Trp beta15, demonstrating that Trp beta37 plays a pivotal role in the quaternary structural change in Hb A.

X射线晶体学研究表明，脱氧血红蛋白和配体血红蛋白具有两种不同的四级结构，分别称为T-态和R-态。合作氧合血红蛋白已被解释在两个四级结构之间的可逆过渡部分连接到四个血红素。用紫外共振拉曼光谱（UVRR）和圆二色性（CD）研究了血红蛋白（Hb）四级结构T → R转变过程中酪氨酸（Tyr）和色氨酸（Trp）残基的环境变化。为了表征色氨酸β 37在α_1 β_2界面上由于四级结构转变而引起的光谱变化，将血红蛋白A的UVRR光谱与其中色氨酸β 37被丝氨酸（Ser）取代的血红蛋白Hirose的相应光谱进行了比较。脱氧血红蛋白A和脱氧血红蛋白Hirose之间的差谱仅产生Trp RR带，这被合理地归因于脱氧血红蛋白A中的Trp β 37。氧和脱氧状态下的血红蛋白A-Hb Hirose差谱的比较显示，氧诱导的Trp RR带的变化主要来自Trp β 37，剩余的小部分来自Trp β 15，表明Trp β 37在Hb A四级结构变化中起关键作用。

项目成果

S.Hirota,T.Ogura,K.Ito,M.Nagai,T.Titagawa: "Vibrational assignments of the FeCO unit of CO‐bound heme proteins revisited." Journal of Physical Chemistry. 98. 6652-6660 (1994)

S. Hirota、T. Ogura、K. Ito、M. Nagai、T. Titakawa：“CO 结合血红素蛋白的 FeCO 单元的振动分配。”物理化学杂志 98. 6652-6660 (1994)

Nagai,M.& Kitagawa,T.: "Resonance Raman and circular dichroic spectra of Hemoglobin Hirose(β37Trp→Ser)." Journal of Inorganic Biochemistry. 51. 126 (1993)

Nagai, M. & Kitakawa, T.：“广濑血红蛋白的共振拉曼和圆二向色光谱（β37Trp→Ser）。无机生物化学杂志 51. 126 (1993)。

M.Nagai, T.Kitagawa: "Resonance Raman and circular dichroic spectra of Hemoglobin Hirose (Trp beta37->Ser)" J.lnorg.Biochem.51 (1&2). 126 (1993)

M.Nagai、T.Kitakawa：“广濑血红蛋白的共振拉曼和圆二向色光谱（Trp beta37->Ser）”J.lnorg.Biochem.51（1

T.Lian,B.Locke,T.Kitagawa,M.Nagai,R.M.Hochst: "Determination of Fe‐CO geometry in the subunits of carbon monooxy Hb M Boston using femtosecond infrared spectroscopy." Biochemistry. 32. 5809-5814 (1993)

T. Lian、B. Locke、T. Kitakawa、M. Nagai、R. M. Hochst：“使用飞秒红外光谱法测定单氧碳 Hb M 波士顿亚基中的 Fe-CO 几何形状”32. 5809-5814（1993 年）。 ）

T.Kitagawa,Y.Sakan,M.Nagai,T.Ogura,F.A.Fraunfelter,T.Kitagawa: "Time-resolved resonance Raman studies of recombination intermediates of CO-photodissociated myoglobin,hemoglobin and its E7 mutants." Journal of Inorganic Biochemistry. 51. 217- (1993)

T.Kitakawa、Y.Sakan、M.Nagai、T.Ogura、F.A.Fraunfelter、T.Kitakawa：“CO 光解离肌红蛋白、血红蛋白及其 E7 突变体的重组中间体的时间分辨共振拉曼研究。”