2021 Fiscal Year Final Research Report
Photosynthesis Reaction Mechanism of Photosystem II Protein Studied by Ultrafast Soft X-ray Absorption Spectroscopy
Project/Area Number |
19H02680
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Review Section |
Basic Section 32010:Fundamental physical chemistry-related
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Research Institution | Institute for Molecular Science |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
足立 純一 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 研究機関講師 (10322629)
手老 龍吾 豊橋技術科学大学, 工学(系)研究科(研究院), 准教授 (40390679)
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Project Period (FY) |
2019-04-01 – 2022-03-31
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Keywords | 軟X線吸収分光法 / 光化学系IIタンパク質 / 時間分解測定 / 光合成反応 / 金属錯体 |
Outline of Final Research Achievements |
The purpose of this study is to observe the structure of the oxygen evolving center in the photosystem II (PSII) protein and its molecular interaction with water by using an ultrafast soft X-ray absorption spectroscopy (XAS). We have measured XAS spectra of PSII proteins embedded in lipid bilayers, where PSII proteins are worked as membrane proteins. We have also developed the ultrafast XAS measurement system with the combination of soft X-ray pulses from synchrotron radiation with femto second laser pulses and observed the high spin state of iron phenanthroline complexes with the photoexcitation state by using N K-edge XAS. In the future, we will realize the ultrafast XAS measurement of the PSII protein during the photosynthesis reaction by the combination of our developed techniques.
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Free Research Field |
物理化学
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Academic Significance and Societal Importance of the Research Achievements |
本研究で開発した光化学系II (PSII)タンパク質の軟X線吸収分光(XAS)法により、膜タンパク質の元素・官能基選択的な電子状態解析が実現する。また、光化学反応の超高速XAS法により、その励起状態解析が行えるので、将来的なPSIIタンパク質の光合成反応の機構解明が期待されるため、その学術的な意義は大きい。また、天然の光合成反応の理解に留まらず、光触媒による人工光合成系の開発につながる可能性もあり、その社会的な意義も大きいと考える。
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