Evidence map›Paper›PMID 23469138›Full record

ArticlePloS one2013

Oxidized amino acid residues in the vicinity of Q(A) and Pheo(D1) of the photosystem II reaction center: putative generation sites of reducing-side reactive oxygen species.

Laurie K Frankel, Larry Sallans, Patrick A Limbach, Terry M Bricker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Bicarbonate-controlled reduction of oxygen by the QProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Review
  13. Review
  14. Article
  15. 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

4 authors at 2 institutions in 1 country.

Laurie K FrankelDepartment of Biological Sciences, Division of Biochemistry and Molecular Biology, Louisiana State University, Baton Rouge, Louisiana, United States of America.
Larry Sallans
Patrick A Limbach
Terry M Bricker
Louisiana State University · USUniversity of Cincinnati · US

Funding

UPLC for Enhanced Mass Spectrometry of Modified RNAsR01GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 1999 to 2025
$5.1M
MASS SPECTROMETER: PROTEOMICSS10RR019900 · NCRR · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 2005 to 2005
$919k
Mass Spectrometry of Ribosomal RNA:Protein InteractionsR56GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 2009 to 2009
$330k
NCRR NIH HHS RR019900NCRR NIH HHS S10 RR019900NIGMS NIH HHS GM58843NIGMS NIH HHS R01 GM058843NIGMS NIH HHS R56 GM058843
6 · The paper itself

Abstract

Under a variety of stress conditions, Photosystem II produces reactive oxygen species on both the reducing and oxidizing sides of the photosystem. A number of different sites including the Mn4O5Ca cluster, P680, PheoD1, QA, QB and cytochrome b559 have been hypothesized to produce reactive oxygen species in the photosystem. In this communication using Fourier-transform ion cyclotron resonance mass spectrometry we have identified several residues on the D1 and D2 proteins from spinach which are oxidatively modified and in close proximity to QA (D1 residues (239)F, (241)Q, (242)E and the D2 residues (238)P, (239)T, (242)E and (247)M) and PheoD1 (D1 residues (130)E, (133)L and (135)F). These residues may be associated with reactive oxygen species exit pathways located on the reducing side of the photosystem, and their modification may indicate that both QA and PheoD1 are sources of reactive oxygen species on the reducing side of Photosystem II.

Indexed as

Amino AcidsAmino Acid SequenceCatalytic DomainMass SpectrometryModels, MolecularMolecular Sequence DataOxidation-ReductionPhotosystem II Protein ComplexReactive Oxygen SpeciesSpinacia oleraceaAmino AcidsPhotosystem II Protein ComplexReactive Oxygen Species

Identifiers

PMID23469138
PMCPMC3585169
OpenAlexW2045743530

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.