| Project/Area Number |
16K05850
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Bio-related chemistry
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| Research Institution | Tokyo University of Science, Yamaguchi (2018-2019)
University of Hyogo (2016-2017) |
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Principal Investigator |
OHTA Takehiro 山陽小野田市立山口東京理科大学, 工学部, 准教授 (70509950)
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| Project Period (FY) |
2016-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2018: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 核共鳴非弾性散乱分光 / 共鳴ラマン分光 / ヘム蛋白質 / 気体センサー蛋白質 / ヘムタンパク質 / 酸素結合タンパク質 / 振動分光法 / 共鳴ラマン分光法 / 鉄含有蛋白質 / 振動分光 / 生物物理 / ヘム鉄蛋白質 / 非ヘム鉄蛋白質 / 核共鳴非弾性散乱 / 共鳴ラマン / 金属蛋白質モデル錯体 / 酸素活性化 / センサー蛋白質 / 蛋白質 / シグナル伝達 / 分析科学 |
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| Outline of Final Research Achievements |
Nuclear resonance vibrational spectroscopy (NRVS) was applied to myoglobin. The nature of Fe－O2 bond in oxy Hb and Mb had been extensively investigated by resonance Raman spectroscopy, which assigned the Fe－O2 stretching bands at 570 cm－1. However, resonance Raman assignment of the vibrational mode had been elusive due to the spectroscopic selection rule and to the limited information available about the ground-state molecular structure. NRVS analyses in conjunction with DFT calculations gave new insights into the nature of the Fe－O2 bond of oxy heme by revealing the effect of heme peripheral substitutions on the vibrational dynamics of heme Fe atom, where the main Fe－O2 stretching band of the native protein was characterized at 420 cm－1. Thus, NRVS shed new light on the molecular mechanism of hemproteins that function upon binding of diatomic gas molecules.
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| Academic Significance and Societal Importance of the Research Achievements |
気体分子結合型ヘムの分子構造の解析は、各種ヘム蛋白質の分子機構の解明に重要である。本研究では、放射光施設を利用した核共鳴非弾性散乱分光法 (NRVS) により、ミオグロビンのヘム鉄近傍の分子振動構造解析を行った。酸素結合型ミオグロビンの解析では、ヘム鉄－酸素結合の分子振動構造について、従来の見解とは異なる新たな知見を得た。本成果は、酸素もしくは他の2原子気体分子と相互作用し、分子内情報伝達により機能発現する各種ヘム蛋白質の研究に新たな展開をもたらす。
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