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
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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
Author_xml	– sequence: 1 orcidid: 0000-0002-4880-7300 fullname: 宮﨑直幸 – sequence: 2 orcidid: 0000-0001-9846-5903 fullname: Kato Koji – sequence: 3 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 – sequence: 9 fullname: Allakhverdiev Suleyman I. – sequence: 10 orcidid: 0000-0003-4471-8797 fullname: Shen Jian-Ren – sequence: 11 fullname: Akita Fusamichi – sequence: 12 orcidid: 0000-0002-9369-1941 fullname: Tomo Tatsuya
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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
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Volume	11
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