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Structural basis for the adaptation and function of chlorophyll f in photosystem I
by
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
in
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
2020
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Structural basis for the adaptation and function of chlorophyll f in photosystem I
by
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
in
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
2020
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Structural basis for the adaptation and function of chlorophyll f in photosystem I
by
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
in
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
2020
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Structural basis for the adaptation and function of chlorophyll f in photosystem I
Journal Article
Structural basis for the adaptation and function of chlorophyll f in photosystem I
2020
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Overview
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.
Publisher
Nature,Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/45
/ 82/83
/ Chlorophyll - analogs & derivatives
/ Chlorophyll - radiation effects
/ Chlorophyll A - radiation effects
/ Humanities and Social Sciences
/ Light
/ Photosystem I Protein Complex - chemistry
/ Photosystem I Protein Complex - metabolism
/ Photosystem I Protein Complex - radiation effects
/ Science
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