Evidence map›Paper›PMID 37202365›Full record

ArticlePlant physiology2023

Bicarbonate activation of the monomeric photosystem II-PsbS/Psb27 complex.

Andrea Fantuzzi, Patrycja Haniewicz, Domenica Farci, M Cecilia Loi, Keunha Park, Claudia Büchel, Matthias Bochtler, A William Rutherford, Dario Piano

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2023. 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
2.0field-weighted citation impact, top 14% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification of PsbS binding proteins inFrontiers in plant science · 2025
    Article
  4. Review
  5. 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

9 authors at 6 institutions in 5 countries.

Andrea FantuzziDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.ORCID 0000-0002-7026-2175
Patrycja HaniewiczDepartment of Plant Physiology, Warsaw University of Life Sciences - SGGW, Warsaw 02-776, Poland.ORCID 0000-0002-6298-7184
Domenica FarciDepartment of Chemistry, Umea University, 90187 Umea, Sweden.ORCID 0000-0002-3691-2699
M Cecilia LoiDepartment of Life and Environmental Sciences, University of Cagliari, Cagliari 09123, Italy.ORCID 0000-0002-2708-4019
Keunha ParkDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.ORCID 0009-0006-6984-0990
Claudia BüchelInstitute of Molecular Biosciences, University of Frankfurt, Frankfurt am Main 60438, Germany.ORCID 0000-0001-6640-7610
Matthias BochtlerLaboratory of Structural Biology, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.ORCID 0000-0001-7884-4463
A William RutherfordDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.ORCID 0000-0002-3124-154X
Dario PianoLaboratory of Structural Biology, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.ORCID 0000-0003-2980-7572
Imperial College London · GBUniversity of Cagliari · ITGoethe University Frankfurt · DEInternational Institute of Molecular and Cell Biology · PLUmeå University · SEWarsaw University of Life Sciences · PL

Funding

Biotechnology and Biological Sciences Research Council BB/K002627/1Biotechnology and Biological Sciences Research Council BB/R00921X
6 · The paper itself

Abstract

In thylakoid membranes, photosystem II (PSII) monomers from the stromal lamellae contain the subunits PsbS and Psb27 (PSIIm-S/27), while PSII monomers (PSIIm) from granal regions lack these subunits. Here, we have isolated and characterized these 2 types of PSII complexes in tobacco (Nicotiana tabacum). PSIIm-S/27 showed enhanced fluorescence, the near absence of oxygen evolution, and limited and slow electron transfer from QA to QB compared to the near-normal activities in the granal PSIIm. However, when bicarbonate was added to PSIIm-S/27, water splitting and QA to QB electron transfer rates were comparable to those in granal PSIIm. The findings suggest that the binding of PsbS and/or Psb27 inhibits forward electron transfer and lowers the binding affinity for bicarbonate. This can be rationalized in terms of the recently discovered photoprotection role played by bicarbonate binding via the redox tuning of the QA/QA•- couple, which controls the charge recombination route, and this limits chlorophyll triplet-mediated 1O2 formation. These findings suggest that PSIIm-S/27 is an intermediate in the assembly of PSII in which PsbS and/or Psb27 restrict PSII activity while in transit using a bicarbonate-mediated switch and protective mechanism.

Indexed as

BicarbonatesPhotosystem II Protein ComplexElectron TransportOxidation-ReductionThylakoidsBicarbonatesPhotosystem II Protein Complex

Identifiers

PMID37202365
PMCPMC10400029
OpenAlexW4377014331

What OpenQuestion holds

Textmetadata
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.