Evidence map›Paper›PMID 25692589›Full record

ArticleBiophysical journal2015

Low pH modulates the macroorganization and thermal stability of PSII supercomplexes in grana membranes.

Svetozar Stoichev, Sashka B Krumova, Tonya Andreeva, Jon V Busto, Svetla Todinova, Konstantin Balashev, Mira Busheva, Félix M Goñi, Stefka G Taneva

Abstract read
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Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

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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

9 authors.

Svetozar StoichevInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Sofia, Bulgaria.
Sashka B KrumovaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Sofia, Bulgaria.
Tonya AndreevaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Sofia, Bulgaria.
Jon V BustoUnidad de Biofísica (CSIC, UPV-EHU) and Departamento de Bioquímica, Universidad del País Vasco, Leioa, Spain.
Svetla TodinovaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Sofia, Bulgaria.
Konstantin BalashevDepartment of Physical Chemistry, Faculty of Chemistry and Pharmacy, Sofia University "St. Kliment Ohridski," Sofia, Bulgaria.
Mira BushevaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Sofia, Bulgaria.
Félix M GoñiUnidad de Biofísica (CSIC, UPV-EHU) and Departamento de Bioquímica, Universidad del País Vasco, Leioa, Spain.
Stefka G TanevaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Sofia, Bulgaria; Unidad de Biofísica (CSIC, UPV-EHU) and Departamento de Bioquímica, Universidad del País Vasco, Leioa, Spain. Electronic address: stefka.germanova@ehu.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protonation of the lumen-exposed residues of some photosynthetic complexes in the grana membranes occurs under conditions of high light intensity and triggers a major photoprotection mechanism known as energy dependent nonphotochemical quenching. We have studied the role of protonation in the structural reorganization and thermal stability of isolated grana membranes. The macroorganization of granal membrane fragments in protonated and partly deprotonated state has been mapped by means of atomic force microscopy. The protonation of the photosynthetic complexes has been found to induce large-scale structural remodeling of grana membranes-formation of extensive domains of the major light-harvesting complex of photosystem II and clustering of trimmed photosystem II supercomplexes, thinning of the membrane, and reduction of its size. These events are accompanied by pronounced thermal destabilization of the photosynthetic complexes, as evidenced by circular dichroism spectroscopy and differential scanning calorimetry. Our data reveal a detailed nanoscopic picture of the initial steps of nonphotochemical quenching.

Indexed as

Enzyme StabilityHot TemperatureHydrogen-Ion ConcentrationPhotosystem II Protein ComplexPisum sativumProtein DenaturationThylakoidsPhotosystem II Protein Complex

Identifiers

PMID25692589
PMCPMC4336371

What OpenQuestion holds

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Registered trials

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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.