Evidence map›Paper›PMID 36514981›Full record

ReviewOpen biology2022

Light-induced reversible reorganizations in closed Type II reaction centre complexes: physiological roles and physical mechanisms.

G Sipka, L Nagy, M Magyar, P Akhtar, J-R Shen, A R Holzwarth, P H Lambrev, G Garab

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Revisiting the QPhotosynthesis research · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Letter to the Editor.Photosynthetica · 2024
    Article
  6. Article
  7. Article
  8. 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

8 authors at 5 institutions in 5 countries.

G SipkaInstitute of Plant Biology, Biological Research Centre, Szeged, Temesvári körút 62, 6726 Szeged, Hungary.ORCID 0000-0002-8553-4890
L NagyInstitute of Plant Biology, Biological Research Centre, Szeged, Temesvári körút 62, 6726 Szeged, Hungary.
M MagyarInstitute of Plant Biology, Biological Research Centre, Szeged, Temesvári körút 62, 6726 Szeged, Hungary.ORCID 0000-0002-1144-4657
P AkhtarInstitute of Plant Biology, Biological Research Centre, Szeged, Temesvári körút 62, 6726 Szeged, Hungary.ORCID 0000-0002-3264-7154
J-R ShenInstitute of Interdisciplinary Science, and Graduate School of Natural Science and Technology, Okayama University, 700-8530 Okayama, Japan.
A R HolzwarthMax-Planck-Institute for Chemical Energy Conversion, 45470 Mülheim a.d. Ruhr, Germany.ORCID 0000-0002-9562-4873
P H LambrevInstitute of Plant Biology, Biological Research Centre, Szeged, Temesvári körút 62, 6726 Szeged, Hungary.ORCID 0000-0001-5147-153X
G GarabInstitute of Plant Biology, Biological Research Centre, Szeged, Temesvári körút 62, 6726 Szeged, Hungary.ORCID 0000-0002-3869-9959
HUN-REN Szegedi Biológiai Kutatóközpont · HUMax Planck Institute for Chemical Energy Conversion · DEOkayama University · JPUniversity of Ostrava · CZUniversity of Szeged · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The purpose of this review is to outline our understanding of the nature, mechanism and physiological significance of light-induced reversible reorganizations in closed Type II reaction centre (RC) complexes. In the so-called 'closed' state, purple bacterial RC (bRC) and photosystem II (PSII) RC complexes are incapable of generating additional stable charge separation. Yet, upon continued excitation they display well-discernible changes in their photophysical and photochemical parameters. Substantial stabilization of their charge-separated states has been thoroughly documented-uncovering light-induced reorganizations in closed RCs and revealing their physiological importance in gradually optimizing the operation of the photosynthetic machinery during the dark-to-light transition. A range of subtle light-induced conformational changes has indeed been detected experimentally in different laboratories using different bRC and PSII-containing preparations. In general, the presently available data strongly suggest similar structural dynamics of closed bRC and PSII RC complexes, and similar physical mechanisms, in which dielectric relaxation processes and structural memory effects of proteins are proposed to play important roles.

Indexed as

PhotosynthesisPhotosystem II Protein ComplexPhotosystem II Protein Complexchlorophyll fluorescencedielectric relaxationdynamics and structural memory of proteinsMarcus theoryphotosystem IIpurple bacterial reaction centre

Identifiers

PMID36514981
PMCPMC9748786
OpenAlexW4311380739

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.