ID 55218
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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 ORCID Kakenhi publons
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 Kakenhi publons
Abstract
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
Published Date
2017-03
Publication Title
Nature
Volume
volume543
Issue
issue7643
Publisher
Nature Publishing Group
Start Page
131
End Page
135
ISSN
0028-0836
NCID
AA00752384
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
Copyright Holders
https://creativecommons.org/licenses/by-nc-nd/4.0/deed.ja
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DOI
Web of Science KeyUT
Related Url
https://doi.org/10.1038/nature21400