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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Veröffentlicht in:Nature Communications Jg. 11; H. 1; S. 238 - 10
Hauptverfasser: 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
Sprache:Englisch
Veröffentlicht: London Nature 13.01.2020
Nature Publishing Group UK
Nature Publishing Group
Nature Portfolio
Schlagworte:
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
ISSN:2041-1723, 2041-1723
Online-Zugang:Volltext
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Zusammenfassung: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.
Bibliographie:ObjectType-Article-1
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ObjectType-Feature-2
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ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-019-13898-5