ID | 58228 |
フルテキストURL | |
著者 |
Kato, Koji
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Shinoda, Toshiyuki
Faculty of Science, Tokyo University of Science
Nagao, Ryo
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Akimoto, Seiji
Graduate School of Science, Kobe University
Suzuki, Takehiro
Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Dohmae, Naoshi
Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Chen, Min
School of Life and Environmental Sciences, University of Sydney
Allakhverdiev, Suleyman I.
K.A. Timiryazev Institute of Plant Physiology RAS
Shen, Jian-Ren
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
ORCID
Kaken ID
publons
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Akita, Fusamichi
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
ORCID
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Miyazaki, Naoyuki
Institute for Protein Research, Laboratory of Protein Synthesis and Expression, Osaka University
Tomo, Tatsuya
Faculty of Science, Tokyo University of Science
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抄録 | Chlorophylls (Chl) play pivotal roles in energy capture, transfer and charge separation in photosynthesis. Among Chls functioning in oxygenic photosynthesis, Chl f is the most red-shifted type first found in a cyanobacterium Halomicronema hongdechloris. The location and function of Chl f in photosystems are not clear. Here we analyzed the high-resolution structures of photosystem I (PSI) core from H. hongdechloris grown under white or far-red light by cryo-electron microscopy. The structure showed that, far-red PSI binds 83 Chl a and 7 Chl f, and Chl f are associated at the periphery of PSI but not in the electron transfer chain. The appearance of Chl f is well correlated with the expression of PSI genes induced under far-red light. These results indicate that Chl f functions to harvest the far-red light and enhance uphill energy transfer, and changes in the gene sequences are essential for the binding of Chl f.
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発行日 | 2020-01-13
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出版物タイトル |
Nature Communications
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巻 | 11巻
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号 | 1号
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出版者 | Nature Research
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開始ページ | 238
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ISSN | 2041-1723
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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 | © The Author(s) 2020
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論文のバージョン | publisher
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PubMed ID | |
DOI | |
Web of Science KeyUT | |
関連URL | isVersionOf https://doi.org/10.1038/s41467-019-13898-5
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ライセンス | http://creativecommons.org/licenses/by/4.0/
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助成機関名 |
日本学術振興会
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助成番号 | 17K07442
19H04726
17H06434
17726220801
17K07453
18H05177
19K22396
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