Evidence map›Paper›PMID 23277574›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Mechanism of proton-coupled quinone reduction in Photosystem II.

Keisuke Saito, A William Rutherford, Hiroshi Ishikita

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

64 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
  2. The contribution of thePhotosynthesis research · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Iron mobilization from intact ferritin: effect of differential redox activity of quinone derivatives with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  13. Article
  14. Rotaxane-Functionalized Dyes for Charge-Rectification in p-Type Photoelectrochemical Devices.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  15. Review
  16. Article
  17. Photocatalytic CONature communications · 2023
    Article
  18. Functional Water Networks in Fully Hydrated Photosystem II.Journal of the American Chemical Society · 2022
    Article
  19. Article
  20. Article

4 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

3 authors at 2 institutions in 2 countries.

Keisuke SaitoCareer-Path Promotion Unit for Young Life Scientists, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan.
A William Rutherford
Hiroshi Ishikita
Japan Science and Technology Agency · JPImperial College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosystem II uses light to drive water oxidation and plastoquinone (PQ) reduction. PQ reduction involves two PQ cofactors, Q(A) and Q(B), working in series. Q(A) is a one-electron carrier, whereas Q(B) undergoes sequential reduction and protonation to form Q(B)H(2). Q(B)H(2) exchanges with PQ from the pool in the membrane. Based on the atomic coordinates of the Photosystem II crystal structure, we analyzed the proton transfer (PT) energetics adopting a quantum mechanical/molecular mechanical approach. The potential-energy profile suggests that the initial PT to Q(B)(•-) occurs from the protonated, D1-His252 to Q(B)(•)(-) via D1-Ser264. The second PT is likely to occur from D1-His215 to Q(B)H(-) via an H-bond with an energy profile with a single well, resulting in the formation of Q(B)H(2) and the D1-His215 anion. The pathway for reprotonation of D1-His215(-) may involve bicarbonate, D1-Tyr246 and water in the Q(B) site. Formate ligation to Fe(2+) did not significantly affect the protonation of reduced Q(B), suggesting that formate inhibits Q(B)H(2) release rather than its formation. The presence of carbonate rather than bicarbonate seems unlikely because the calculations showed that this greatly perturbed the potential of the nonheme iron, stabilizing the Fe(3+) state in the presence of Q(B)(•-), a situation not encountered experimentally. H-bonding from D1-Tyr246 and D2-Tyr244 to the bicarbonate ligand of the nonheme iron contributes to the stability of the semiquinones. A detailed mechanistic model for Q(B) reduction is presented.

Indexed as

BicarbonatesBinding SitesCrystallography, X-RayCyanobacteriaElectron TransportHydrogen BondingLigandsModels, MolecularOxidation-ReductionPhotosystem II Protein ComplexProtonsQuantum TheoryQuinonesStatic ElectricityThermodynamicsTyrosineBicarbonatesLigandsPhotosystem II Protein ComplexProtonsQuinonesTyrosine

Identifiers

PMID23277574
PMCPMC3549079
OpenAlexW2130138576

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.