Evidence map›Paper›PMID 31932639›Full record

ArticleNature communications2020

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

Koji Kato, Toshiyuki Shinoda, Ryo Nagao, Seiji Akimoto, Takehiro Suzuki, Naoshi Dohmae, Min Chen, Suleyman I Allakhverdiev, Jian-Ren Shen, Fusamichi Akita and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
6.3field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 130 citations in OpenAlex.

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  15. Two new non-chlorophyllFrontiers in microbiology · 2025
    Article
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  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 7 institutions in 4 countries.

Koji KatoResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.
Toshiyuki ShinodaFaculty of Science, Tokyo University of Science, Tokyo, 162-8601, Japan.
Ryo NagaoResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.
Seiji AkimotoGraduate School of Science, Kobe University, Kobe, 657-8501, Japan.ORCID http://orcid.org/0000-0002-8951-8978
Takehiro SuzukiBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Min ChenSchool of Life and Environmental Sciences, University of Sydney, Sydney, Australia.ORCID http://orcid.org/0000-0001-8070-3248
Suleyman I AllakhverdievK.A. Timiryazev Institute of Plant Physiology RAS, Moscow, Russia.ORCID http://orcid.org/0000-0002-0452-232X
Jian-Ren ShenResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan. shen@okayama-u.ac.jp.ORCID http://orcid.org/0000-0003-4471-8797
Fusamichi AkitaResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan. fusamichi_a@okayama-u.ac.jp.ORCID http://orcid.org/0000-0003-0537-6157
Naoyuki MiyazakiInstitute for Protein Research, Laboratory of Protein Synthesis and Expression, Osaka University, Osaka, 565-0871, Japan. naomiyazaki@tara.tsukuba.ac.jp.ORCID http://orcid.org/0000-0002-4880-7300
Tatsuya TomoFaculty of Science, Tokyo University of Science, Tokyo, 162-8601, Japan. tomo@rs.tus.ac.jp.ORCID http://orcid.org/0000-0002-9369-1941
Okayama University of Science · JPRIKEN Center for Sustainable Resource Science · JPTokyo University of Science · JPAzerbaijan National Academy of Sciences · AZKobe University · JPThe University of Sydney · AUUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Binding SitesChlorophyllChlorophyll ACryoelectron MicroscopyCyanobacteriaEnergy TransferLightModels, MolecularPhotosystem I Protein ComplexProtein ConformationChlorophyllChlorophyll Achlorophyll fPhotosystem I Protein Complex

Identifiers

PMID31932639
PMCPMC6957486
OpenAlexW2999824576

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.