Evidence map›Paper›PMID 26715751›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Redox potential of the terminal quinone electron acceptor QB in photosystem II reveals the mechanism of electron transfer regulation.

Yuki Kato, Ryo Nagao, Takumi Noguchi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 77 citations in OpenAlex.

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  7. Illuminating the coevolution of photosynthesis and Bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  17. Acquirement of water-splitting ability and alteration of the charge-separation mechanism in photosynthetic reaction centers.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  18. Article
  19. Energetics of the exchangeable quinone, QProceedings of the National Academy of Sciences of the United States of America · 2019
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  20. Article
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

3 authors at 1 institution in 2 countries.

Yuki KatoDivision of Material Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan yuki.kato@bio.phys.nagoya-u.ac.jp tnoguchi@bio.phys.nagoya-u.ac.jp.
Ryo NagaoDivision of Material Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Takumi NoguchiDivision of Material Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan yuki.kato@bio.phys.nagoya-u.ac.jp tnoguchi@bio.phys.nagoya-u.ac.jp.
Institut de Biologie Physico-Chimique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosystem II (PSII) extracts electrons from water at a Mn4CaO5 cluster using light energy and then transfers them to two plastoquinones, the primary quinone electron acceptor QA and the secondary quinone electron acceptor QB. This forward electron transfer is an essential process in light energy conversion. Meanwhile, backward electron transfer is also significant in photoprotection of PSII proteins. Modulation of the redox potential (Em) gap of QA and QB mainly regulates the forward and backward electron transfers in PSII. However, the full scheme of electron transfer regulation remains unresolved due to the unknown Em value of QB. Here, for the first time (to our knowledge), the Em value of QB reduction was measured directly using spectroelectrochemistry in combination with light-induced Fourier transform infrared difference spectroscopy. The Em(QB (-)/QB) was determined to be approximately +90 mV and was virtually unaffected by depletion of the Mn4CaO5 cluster. This insensitivity of Em(QB (-)/QB), in combination with the known large upshift of Em(QA (-)/QA), explains the mechanism of PSII photoprotection with an impaired Mn4CaO5 cluster, in which a large decrease in the Em gap between QA and QB promotes rapid charge recombination via QA (-).

Indexed as

ElectronsComputer SimulationElectrodesElectron TransportManganeseModels, MolecularOxidation-ReductionPhotosystem II Protein ComplexQuinonesSpectroscopy, Fourier Transform InfraredThermodynamicsManganesePhotosystem II Protein ComplexQuinonesFTIRphotosynthesisspectroelectrochemistry

Identifiers

PMID26715751
PMCPMC4725517
OpenAlexW2198491797

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.