Structural basis for the adaptation and function of chlorophyll f in photosystem I

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 photosys...

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Published in:Nature Communications Vol. 11; no. 1; pp. 238 - 10
Main Authors: 宮﨑 直幸, Kato Koji, Shinoda Toshiyuki, Nagao Ryo, Akimoto Seiji, Suzuki Takehiro, Dohmae Naoshi, Chen Min, Allakhverdiev Suleyman I., Shen Jian-Ren, Akita Fusamichi, Tomo Tatsuya
Format: Journal Article
Language:English
Published: London Nature 13.01.2020
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ISSN:2041-1723, 2041-1723
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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.
AbstractList 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.Chlorophyll f (Chl f) is the most red-shifted Chl in oxygenic photosynthesis but its localization in photosystem I (PSI) has been unknown so far. Here the authors determine the cryo-EM structures of PSI complexes from a Chl f-containing cyanobacterium grown either under white light or far-red light conditions and identify seven Chls f in the far-red light PSI structure, whereas PSI from cells grown under white light contains only Chl a.
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 .
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.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.
Chlorophyll f (Chl f) is the most red-shifted Chl in oxygenic photosynthesis but its localization in photosystem I (PSI) has been unknown so far. Here the authors determine the cryo-EM structures of PSI complexes from a Chl f-containing cyanobacterium grown either under white light or far-red light conditions and identify seven Chls f in the far-red light PSI structure, whereas PSI from cells grown under white light contains only Chl a.
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.
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 . Chlorophyll f (Chl f ) is the most red-shifted Chl in oxygenic photosynthesis but its localization in photosystem I (PSI) has been unknown so far. Here the authors determine the cryo-EM structures of PSI complexes from a Chl f -containing cyanobacterium grown either under white light or far-red light conditions and identify seven Chls f in the far-red light PSI structure, whereas PSI from cells grown under white light contains only Chl a .
ArticleNumber 238
Author Kato Koji
Shen Jian-Ren
Shinoda Toshiyuki
Nagao Ryo
Suzuki Takehiro
Dohmae Naoshi
Akita Fusamichi
Akimoto Seiji
Tomo Tatsuya
宮﨑 直幸
Allakhverdiev Suleyman I.
Chen Min
Author_FL MIYAZAKI Naoyuki
Author_FL_xml – sequence: 1
  fullname: MIYAZAKI Naoyuki
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  orcidid: 0000-0001-9846-5903
  fullname: Kato Koji
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  fullname: Shinoda Toshiyuki
– sequence: 4
  fullname: Nagao Ryo
– sequence: 5
  fullname: Akimoto Seiji
– sequence: 6
  orcidid: 0000-0002-0585-6305
  fullname: Suzuki Takehiro
– sequence: 7
  fullname: Dohmae Naoshi
– sequence: 8
  fullname: Chen Min
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  fullname: Allakhverdiev Suleyman I.
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  orcidid: 0000-0003-4471-8797
  fullname: Shen Jian-Ren
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  fullname: Akita Fusamichi
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  fullname: Tomo Tatsuya
BackLink https://cir.nii.ac.jp/crid/1570572702665896320$$DView record in CiNii
https://www.ncbi.nlm.nih.gov/pubmed/31932639$$D View this record in MEDLINE/PubMed
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Snippet Chlorophylls (Chl) play pivotal roles in energy capture, transfer and charge separation in photosynthesis. Among Chls functioning in oxygenic photosynthesis,...
Chlorophyll f (Chl f) is the most red-shifted Chl in oxygenic photosynthesis but its localization in photosystem I (PSI) has been unknown so far. Here the...
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SubjectTerms 101/28
631/449/1734/2075
631/45
631/535/1258/1259
82/83
Binding Sites
Charge transfer
Chlorophyll
Chlorophyll - analogs & derivatives
Chlorophyll - metabolism
Chlorophyll - radiation effects
Chlorophyll A - metabolism
Chlorophyll A - radiation effects
Cryoelectron Microscopy
Cyanobacteria - chemistry
Cyanobacteria - physiology
Electron microscopy
Electron transfer
Energy charge
Energy Transfer
Gene expression
Gene sequencing
Humanities and Social Sciences
Light
Localization
Models, Molecular
multidisciplinary
Photosynthesis
Photosystem I
Photosystem I Protein Complex - chemistry
Photosystem I Protein Complex - metabolism
Photosystem I Protein Complex - radiation effects
Protein Conformation
Science
Science (multidisciplinary)
White light
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Title Structural basis for the adaptation and function of chlorophyll f in photosystem I
URI https://cir.nii.ac.jp/crid/1570572702665896320
https://link.springer.com/article/10.1038/s41467-019-13898-5
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