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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Vydané v:	Nature Communications Ročník 11; číslo 1; s. 238 - 10
Hlavní autori:	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
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature 13.01.2020 Nature Publishing Group UK Nature Publishing Group Nature Portfolio
Predmet:	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
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Shrnutí:	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.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	2041-1723 2041-1723
DOI:	10.1038/s41467-019-13898-5