Evidence map›Paper›PMID 23814046›Full record

ArticleThe Journal of biological chemistry2013

Radiolytic mapping of solvent-contact surfaces in Photosystem II of higher plants: experimental identification of putative water channels within the photosystem.

Laurie K Frankel, Larry Sallans, Henry Bellamy, Jost S Goettert, Patrick A Limbach, Terry M Bricker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 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
2.2field-weighted citation impact, top 12% 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, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. 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
  10. Review
  11. Article
  12. X-ray radiation-induced addition of oxygen atoms to protein residues.Protein science : a publication of the Protein Society · 2016
    Article
  13. Review
  14. Local and global structural drivers for the photoactivation of the orange carotenoid protein.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

6 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 70803, USA.
Larry Sallans
Henry Bellamy
Jost S Goettert
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

Photosystem II uses water as an enzymatic substrate. It has been hypothesized that this water is vectored to the active site for water oxidation via water channels that lead from the surface of the protein complex to the Mn4O5Ca metal cluster. The radiolysis of water by synchrotron radiation produces amino acid residue-modifying OH(•) and is a powerful technique to identify regions of proteins that are in contact with water. In this study, we have used this technique to oxidatively modify buried amino acid residues in higher plant Photosystem II membranes. Fourier transform ion cyclotron resonance mass spectrometry was then used to identify these oxidized amino acid residues that were located in several core Photosystem II subunits (D1, D2, CP43, and CP47). While, as expected, the majority of the identified oxidized residues (≈75%) are located on the solvent-exposed surface of the complex, a number of buried residues on these proteins were also modified. These residues form groups which appear to lead from the surface of the complex to the Mn4O5Ca cluster. These residues may be in contact with putative water channels in the photosystem. These results are discussed within the context of a number of largely computational studies that have identified putative water channels in Photosystem II.

Indexed as

Mass SpectrometryPeptide MappingPhotosystem II Protein ComplexSpinacia oleraceaWaterPhotosystem II Protein ComplexWaterMass Spectrometry (MS)Membrane EnzymesMembrane ProteinsPhotosynthesisPhotosystem II

Identifiers

PMID23814046
PMCPMC3949330
OpenAlexW2076114460

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.