Evidence map›Paper›PMID 22827410›Full record

ArticleBiochemistry2012

Identification of oxidized amino acid residues in the vicinity of the Mn(4)CaO(5) cluster of Photosystem II: implications for the identification of oxygen channels within the Photosystem.

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

Abstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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. Article
  9. Article
  10. Article
  11. Article
  12. 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
  13. Review
  14. X-ray radiation-induced addition of oxygen atoms to protein residues.Protein science : a publication of the Protein Society · 2016
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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, LA 70803, USA.
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

As a light-driven water-plastoquinone oxidoreductase, Photosystem II produces molecular oxygen as an enzymatic product. Additionally, under a variety of stress conditions, reactive oxygen species are produced at or near the active site for oxygen evolution. In this study, Fourier-transform ion cyclotron resonance mass spectrometry was used to identify oxidized amino acid residues located in several core Photosystem II proteins (D1, D2, CP43, and CP47) isolated from spinach Photosystem II membranes. While the majority of these oxidized residues (81%) are located on the oxygenated solvent-exposed surface of the complex, several residues on the CP43 protein ((354)E, (355)T, (356)M, and (357)R) which are in close proximity (<15 Å) to the Mn(4)CaO(5) active site are also modified. These residues appear to be associated with putative oxygen/reactive oxygen species exit channel(s) in the photosystem. These results are discussed within the context of a number of computational studies which have identified putative oxygen channels within the photosystem.

Indexed as

Amino AcidsCalciumCatalytic DomainFourier AnalysisManganeseMass SpectrometryModels, MolecularOxidation-ReductionOxygenPhotosystem II Protein ComplexPlant ProteinsReactive Oxygen SpeciesSpinacia oleraceaAmino AcidsCalciumManganeseOxygenPhotosystem II Protein ComplexPlant ProteinsReactive Oxygen Species

Identifiers

PMID22827410
PMCPMC3448023
OpenAlexW2070675485

What OpenQuestion holds

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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.