Evidence map›Paper›PMID 18830685›Full record

ReviewPhotosynthesis research

Photosystem II: The machinery of photosynthetic water splitting.

Gernot Renger, Thomas Renger

Abstract readReview
PubMed Publisher
In one paragraph

Review in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing 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

67 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Unveiling the charge transport blockade in the D2 branch of the photosystem II reaction center.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Assignment of the slowly exchanging substrate water of nature's water-splitting cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Natural photoredox catalysts promote light-driven lytic polysaccharide monooxygenase reactions and enzymatic turnover of biomass.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

7 more citing papers are in PubMed but not listed here.

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

2 authors.

Gernot RengerMax Volmer Laboratory for Biophysical Chemistry, Berlin Institute of Technology, Berlin, Germany. rengsbbc@mailbox.tu-berlin.de
Thomas Renger

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This review summarizes our current state of knowledge on the structural organization and functional pattern of photosynthetic water splitting in the multimeric Photosystem II (PS II) complex, which acts as a light-driven water: plastoquinone-oxidoreductase. The overall process comprises three types of reaction sequences: (1) photon absorption and excited singlet state trapping by charge separation leading to the ion radical pair [Formula: see text] formation, (2) oxidative water splitting into four protons and molecular dioxygen at the water oxidizing complex (WOC) with P680+* as driving force and tyrosine Y(Z) as intermediary redox carrier, and (3) reduction of plastoquinone to plastoquinol at the special Q(B) binding site with Q(A)-* acting as reductant. Based on recent progress in structure analysis and using new theoretical approaches the mechanism of reaction sequence (1) is discussed with special emphasis on the excited energy transfer pathways and the sequence of charge transfer steps: [Formula: see text] where (1)(RC-PC)* denotes the excited singlet state (1)P680* of the reaction centre pigment complex. The structure of the catalytic Mn(4)O(X)Ca cluster of the WOC and the four step reaction sequence leading to oxidative water splitting are described and problems arising for the electronic configuration, in particular for the nature of redox state S(3), are discussed. The unravelling of the mode of O-O bond formation is of key relevance for understanding the mechanism of the process. This problem is not yet solved. A multistate model is proposed for S(3) and the functional role of proton shifts and hydrogen bond network(s) is emphasized. Analogously, the structure of the Q(B) site for PQ reduction to PQH(2) and the energetic and kinetics of the two step redox reaction sequence are described. Furthermore, the relevance of the protein dynamics and the role of water molecules for its flexibility are briefly outlined. We end this review by presenting future perspectives on the water oxidation process.

Indexed as

PhotosynthesisKineticsLightOxygenPhotosystem II Protein ComplexPlastoquinoneWaterOxygenPhotosystem II Protein ComplexplastoquinolPlastoquinoneWater

Identifiers

What OpenQuestion holds

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Read underepoch 390

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.