このエントリーをはてなブックマークに追加
ID 58228
FullText URL
fulltext.pdf 3.41 MB
Author
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 researchmap
Akita, Fusamichi Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID publons researchmap
Miyazaki, Naoyuki Institute for Protein Research, Laboratory of Protein Synthesis and Expression, Osaka University
Tomo, Tatsuya Faculty of Science, Tokyo University of Science
Abstract
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.
Published Date
2020-01-13
Publication Title
Nature Communications
Volume
volume11
Issue
issue1
Publisher
Nature Research
Start Page
238
ISSN
2041-1723
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
Copyright Holders
© The Author(s) 2020
File Version
publisher
PubMed ID
DOI
Web of Science KeyUT
Related Url
isVersionOf https://doi.org/10.1038/s41467-019-13898-5
License
http://creativecommons.org/licenses/by/4.0/
Funder Name
Japan Society for the Promotion of Science
助成番号
17K07442
19H04726
17H06434
17726220801
17K07453
18H05177
19K22396