Evidence map›Paper›PMID 23775073›Full record

ArticleThe Journal of biological chemistry2013

A reaction center-dependent photoprotection mechanism in a highly robust photosystem II from an extremophilic red alga, Cyanidioschyzon merolae.

Tomasz Krupnik, Eva Kotabová, Laura S van Bezouwen, Radoslaw Mazur, Maciej Garstka, Peter J Nixon, James Barber, Radek Kaňa, Egbert J Boekema, Joanna Kargul

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 65 citations in OpenAlex.

  1. Excitonic energy transfer in red algal Photosystem I reveals an evolutionary bridge between cyanobacteria and plants.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  20. The CytochromeThe Plant cell · 2019
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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

10 authors at 5 institutions in 4 countries.

Tomasz KrupnikDepartment of Plant Molecular Physiology, Faculty of Biology, University of Warsaw, Miecznikowa 1, 02-096 Warsaw, Poland.
Eva Kotabová
Laura S van Bezouwen
Radoslaw Mazur
Maciej Garstka
Peter J Nixon
James Barber
Radek Kaňa
Egbert J Boekema
Joanna Kargul
University of Warsaw · PLElectron (Ukraine) · UAImperial College London · GBCzech Academy of Sciences · CZCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

Biotechnology and Biological Sciences Research Council BB/C507037/1
6 · The paper itself

Abstract

Members of the rhodophytan order Cyanidiales are unique among phototrophs in their ability to live in extremely low pH levels and moderately high temperatures. The photosynthetic apparatus of the red alga Cyanidioschyzon merolae represents an intermediate type between cyanobacteria and higher plants, suggesting that this alga may provide the evolutionary link between prokaryotic and eukaryotic phototrophs. Although we now have a detailed structural model of photosystem II (PSII) from cyanobacteria at an atomic resolution, no corresponding structure of the eukaryotic PSII complex has been published to date. Here we report the isolation and characterization of a highly active and robust dimeric PSII complex from C. merolae. We show that this complex is highly stable across a range of extreme light, temperature, and pH conditions. By measuring fluorescence quenching properties of the isolated C. merolae PSII complex, we provide the first direct evidence of pH-dependent non-photochemical quenching in the red algal PSII reaction center. This type of quenching, together with high zeaxanthin content, appears to underlie photoprotection mechanisms that are efficiently employed by this robust natural water-splitting complex under excess irradiance. In order to provide structural details of this eukaryotic form of PSII, we have employed electron microscopy and single particle analyses to obtain a 17 Å map of the C. merolae PSII dimer in which we locate the position of the protein mass corresponding to the additional extrinsic protein stabilizing the oxygen-evolving complex, PsbQ'. We conclude that this lumenal subunit is present in the vicinity of the CP43 protein, close to the membrane plane.

Indexed as

Enzyme StabilityHot TemperatureHydrogen-Ion ConcentrationLightPeptide MappingPhotosystem II Protein ComplexRhodophytaPhotosystem II Protein ComplexAlgaeCyanidoschyzon merolaeFluorescencePhotoprotectionPhotosynthesisPhotosynthetic PigmentsPhotosystem IISingle Particle Analysis

Identifiers

PMID23775073
PMCPMC5395030
OpenAlexW2090052787

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.