ID | 55218 |
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著者 |
Suga, Michihiro
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Akita, Fusamichi
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Sugahara, Michihiro
RIKEN SPring-8 Center
Kubo, Minoru
Japan Science and Technology Agency, PRESTO
Nakajima, Yoshiki
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Nakane, Takanori
Department of Biological Sciences, Graduate School of Science, The University of Tokyo
Yamashita, Keitaro
RIKEN SPring-8 Center
Umena, Yasufumi
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Nakabayashi, Makoto
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Yamane, Takahiro
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Nakano, Takamitsu
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Suzuki, Mamoru
Institute for Protein Research, Osaka University
Masuda, Tetsuya
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
Inoue, Shigeyuki
Department of Cell Biology and Anatomy, Graduate School of Medicine, The University of Tokyo
Kimura, Tetsunari
Department of Chemistry, Graduate School of Science, Kobe University
Nomura, Takashi
RIKEN SPring-8 Center
Yonekura, Shinichiro
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Yu, Long-Jiang
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Sakamoto, Tomohiro
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Motomura, Taiki
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Chen, Jing-Hua
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Kato, Yuki
Division of Material Science, Graduate School of Science, Nagoya University
Noguchi, Takumi
Division of Material Science, Graduate School of Science, Nagoya University
Tono, Kensuke
Japan Synchrotron Radiation Research Institute
Joti, Yasumasa
Japan Synchrotron Radiation Research Institute
Kameshima, Takashi
Japan Synchrotron Radiation Research Institute46
Hatsui, Takaki
RIKEN SPring-8 Center
Nango, Eriko
RIKEN SPring-8 Center
Tanaka, Rie
RIKEN SPring-8 Center
Naitow, Hisashi
RIKEN SPring-8 Center
Matsuura, Yoshinori
RIKEN SPring-8 Center
Yamashita, Ayumi
RIKEN SPring-8 Center
Yamamoto, Masaki
RIKEN SPring-8 Center
Nureki, Osamu
Department of Biological Sciences, Graduate School of Science, The University of Tokyo
Yabashi, Makina
RIKEN SPring-8 Center
Ishikawa, Tetsuya
RIKEN SPring-8 Center
Iwata, So
RIKEN SPring-8 Center
Shen, Jian-Ren
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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抄録 | Photosystem II (PSII) is a huge membrane-protein complex consisting of 20 different subunits with a total molecular mass of 350 kDa for a monomer. It catalyses light-driven water oxidation at its catalytic centre, the oxygen-evolving complex (OEC). The structure of PSII has been analysed at 1.9 Å resolution by synchrotron radiation X-rays, which revealed that the OEC is a Mn4CaO5 cluster organized in an asymmetric, 'distorted-chair' form. This structure was further analysed with femtosecond X-ray free electron lasers (XFEL), providing the 'radiation damage-free' structure. The mechanism of O=O bond formation, however, remains obscure owing to the lack of intermediate-state structures. Here we describe the structural changes in PSII induced by two-flash illumination at room temperature at a resolution of 2.35 Å using time-resolved serial femtosecond crystallography with an XFEL provided by the SPring-8 ångström compact free-electron laser. An isomorphous difference Fourier map between the two-flash and dark-adapted states revealed two areas of apparent changes: around the QB/non-haem iron and the Mn4CaO5 cluster. The changes around the QB/non-haem iron region reflected the electron and proton transfers induced by the two-flash illumination. In the region around the OEC, a water molecule located 3.5 Å from the Mn4CaO5 cluster disappeared from the map upon two-flash illumination. This reduced the distance between another water molecule and the oxygen atom O4, suggesting that proton transfer also occurred. Importantly, the two-flash-minus-dark isomorphous difference Fourier map showed an apparent positive peak around O5, a unique μ4-oxo-bridge located in the quasi-centre of Mn1 and Mn4 (refs 4,5). This suggests the insertion of a new oxygen atom (O6) close to O5, providing an O=O distance of 1.5 Å between these two oxygen atoms. This provides a mechanism for the O=O bond formation consistent with that proposed previously
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発行日 | 2017-03
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出版物タイトル |
Nature
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巻 | 543巻
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号 | 7643号
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出版者 | Nature Publishing Group
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開始ページ | 131
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終了ページ | 135
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ISSN | 0028-0836
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NCID | AA00752384
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資料タイプ |
学術雑誌論文
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言語 |
英語
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OAI-PMH Set |
岡山大学
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著作権者 | https://creativecommons.org/licenses/by-nc-nd/4.0/deed.ja
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論文のバージョン | author
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PubMed ID | |
DOI | |
Web of Science KeyUT | |
関連URL | https://doi.org/10.1038/nature21400
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