| Project/Area Number |
15K07026
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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 |
Biophysics
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| Research Institution | Osaka University |
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Principal Investigator |
Oh-oka Hirozo 大阪大学, 理学研究科, 准教授 (30201966)
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| Research Collaborator |
Itoh Shigeru
Kurisu Genji
Azai Chihiro
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 光合成 / 反応中心 / ホモダイマー / ヘリオバクテリア / 光化学系 I / 電子スピン共鳴 / X線結晶構造解析 / ラジカルペア / ESR / スピン分極 / FeSタンパク質 / 初期電荷分離 / 電子伝達 / 緑色イオウ細菌 / タイプ１反応中心 |
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| Outline of Final Research Achievements |
Light-dependent charge separation in photosynthesis is driven by the reaction center (RC) membrane protein complex that is classified into four types; the green bacterial or heliobacterial, the purple bacterial, the photosystem (PS) I and II RCs. Compared to the latter three types of RCs, the molecular architecture of heliobacterial RC is still poorly understood, in part due to the lack of high-resolution structural information. Structure of the RC from Heliobacterium modesticaldum has been solved to a resolution of 3.2 angstrom. Although the X-ray structure, which was reported by Arizona group in 2017, contained no quinone molecule within its, our crystal structure has indicated that it was contained and seemed to function as a secondary acceptor A1. The ESP-EPR signals, which was derived from the charge separated state of P800+A1-, suggested that the quinone molecule had an almost similar orientation to but a little bit different location from that in PS I.
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