TY - JOUR
T1 - Structural basis for the adaptation and function of chlorophyll f in photosystem I
AU - Kato, Koji
AU - Shinoda, Toshiyuki
AU - Nagao, Ryo
AU - Akimoto, Seiji
AU - Suzuki, Takehiro
AU - Dohmae, Naoshi
AU - Chen, Min
AU - Allakhverdiev, Suleyman
AU - Shen, Jian Ren
AU - Akita, Fusamichi
AU - Miyazaki, Naoyuki
AU - Tomo, Tatsuya
N1 - Funding Information:
This work was supported by the Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from AMED (to N.M.), PRESTO from JST Grant No JPMJPR16P1 (to F.A.), JSPS KAKENHI No. JP17K07442, JP19H04726 (to R.N.), JP17H06434 (to J.-R.S.), No. 17726220801, 17K07453, 18H05177 (to T.T.), JP19K22396 (to F.A.). S.I.A., S.A., T.T. and J.-R.S. gratefully acknowledge the JSPS-RFBR grant (No. 19-54-50002). T.T. would like to thank Prof. T. Noguchi for valuable discussion.
Publisher Copyright:
© 2020, The Author(s).
PY - 2020/12/1
Y1 - 2020/12/1
N2 - 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.
AB - 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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U2 - 10.1038/s41467-019-13898-5
DO - 10.1038/s41467-019-13898-5
M3 - Article
C2 - 31932639
AN - SCOPUS:85077786261
SN - 2041-1723
VL - 11
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 238
ER -