| Project/Area Number |
20K22642
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Multi-year Fund |
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| Review Section |
0701:Biology at molecular to cellular levels, and related fields
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| Research Institution | Tokyo Medical and Dental University (2021-2023)
National Institutes for Quantum and Radiological Science and Technology (2020) |
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Principal Investigator |
Hanazono Yuya 東京医科歯科大学, 難治疾患研究所, 准教授 (00750465)
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| Project Period (FY) |
2020-09-11 – 2024-03-31
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| Project Status |
Completed (Fiscal Year 2023)
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| Budget Amount *help |
¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2021: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2020: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | 電子伝達タンパク質 / 精密構造解析 / 中性子構造解析 / X線構造解析 |
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| Outline of Research at the Start |
高電位鉄硫黄タンパク質（HiPIP）の酸化型、還元型二つの状態を高分解能のX線および中性子線回折データをもとに高精度で水素原子を含めた構造解析を行う。高分解能のデータを用いることによって、外角電子の密度形状や電荷、水素原子位置、精密な結合長や結合角を実験的に決定する。さらに、精密な結合長や結合角、相互作用が明らかになった構造から量子化学計算を行うことで、生体中の酸化還元反応のメカニズムを、分子軌道とエネルギー状態から議論する。
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| Outline of Final Research Achievements |
The structural analysis of high-potential iron-sulfur protein derived from Thermochromatium tepidum was performed by combining 0.66 Å resolution X-ray diffraction data and 1.2 Å resolution neutron diffraction data. For the first time, it was successful to refine the coordinates of hydrogen atoms in the protein structure without restraints. Experimentally, it was demonstrated that amide protons, which are thought to exist in the peptide plane, are actually influenced by the surrounding electronic state, showing variability in deviation from planarity. Additionally, the deviation of the amide protons from the plane is also involved in redox functions, suggesting that differences in the peptide planes around the iron-sulfur clusters in oxidized and reduced states contribute to the stabilization of charge states.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究は、高電位鉄硫黄タンパク質構造を、X線および中性子線回折データを用いて高精度で解析し、水素原子の位置を含めた詳細な構造を明らかにしました。この成果は、タンパク質の酸化還元反応のメカニズムを明らかにし、新薬開発や生物工学における応用に貢献します。社会的には、これにより病気の治療法の開発や環境に優しいエネルギー生成方法の研究が進む可能性があります。
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