| Project/Area Number |
16K13933
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Physical chemistry
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| Research Institution | Osaka University |
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Principal Investigator |
Mizuno Misao 大阪大学, 理学研究科, 助教 (10464257)
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| Research Collaborator |
Kawarabata Momoko
Lou Lanqingqing
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| Project Period (FY) |
2016-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | 分子近接場振動分光法 / 共鳴ハイパーラマン散乱 / 分子の対称性 / ヘム / ヘムタンパク質 / 対称中心 / 対称性 / 局所構造観測 / ナノメートル構造 / ダイナミクス観測 |
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| Outline of Final Research Achievements |
We tried to develop a new probe to selectively observe protein dynamics using molecular near-field vibrational spectroscopy. In resonance hyper-Raman processes for centrosymmetric molecules, it was reported that hyper-Raman scattering of their surrounding molecules can be observed due to intermolecular vibronic coupling. Etioheme is a centrosymmetric molecule and can be reconstituted into hemeproteins instead of heme as an intrinsic active site. In etioheme solutions, we were able to observe hyper-Raman scattering of the surroundings, such as solvent molecules and ligated imidazole molecules. These results indicates possibilities of new methodology for measurements of local protein dynamics around the active center in proteins.
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| Academic Significance and Societal Importance of the Research Achievements |
振動分光法をもちいると、サブナノメートルの空間分解能で化学結合の微小変化を検出できます。従来の時間分解共鳴ラマン分光法によるヘムタンパク質の構造ダイナミクス観測では、プローブ部位が、ヘムとその軸配位子であるアミノ酸残基、および芳香族アミノ酸残基に限定されていました。本研究では、第三のダイナミクス観測プローブ部位としてこれまで観測ができなかったヘム周辺のアミノ酸残基の局所構造変化の時間分解計測法を開拓しました。
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