Evidence map›Paper›PMID 18723681›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Photoprotective role of NADPH:protochlorophyllide oxidoreductase A.

Frank Buhr, Majida El Bakkouri, Oscar Valdez, Stephan Pollmann, Nikolai Lebedev, Steffen Reinbothe, Christiane Reinbothe

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Light dependent protochlorophyllide oxidoreductase: a succinct look.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Review
  4. Light controls mesophyll-specific post-transcriptional splicing of photoregulatory genes by AtPRMT5.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Expression ofPlants (Basel, Switzerland) · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

7 authors at 5 institutions in 3 countries.

Frank BuhrLehrstuhl für Pflanzenphysiologie, Universität Bayreuth, Universitätsstrasse 30, D-95447 Bayreuth, Germany.
Majida El Bakkouri
Oscar Valdez
Stephan Pollmann
Nikolai Lebedev
Steffen Reinbothe
Christiane Reinbothe
Centre de Recherches sur les Macromolécules Végétales · FRUniversity of Bayreuth · DERuhr University Bochum · DEUnited States Naval Research Laboratory · USUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A homology model of NADPH:protochlorophyllide (Pchlide) oxidoreductase A (POR; E.C. 1.3.33.1) of barley is developed and verified by site-directed mutagenesis. PORA is considered a globular protein consisting of nine alpha-helices and seven beta-strands. The model predicts the presence of two functionally distinctive Pchlide binding sites where the pigment is coordinated by cysteine residues. The pigment bound to the first, high-affinity Pchlide binding site is used for the formation of the photoactive state of the enzyme. The pigment bound to the second, low-affinity Pchlide binding site is involved in the PORA:PORB interaction, allowing for resonance energy transfer between the neighboring PORs in the complex. In the in vitro reconstituted light-harvesting POR:Pchlide complex (LHPP), light absorbed by PORA-bound Pchlide b is transferred to PORB-bound Pchlide a. That induces the conversion of Pchlide a to chlorophyllide (Chlide) a. This energy transfer eliminates the possibility of Pchlide b photoreduction and prevents that excited triplet states of either Pchlides a or b accumulate and provoke singlet oxygen production. Together, our results provide a photoprotective role of PORA during greening.

Indexed as

Binding SitesEnergy TransferHordeumLightLight-Harvesting Protein ComplexesMutagenesis, Site-DirectedNADH, NADPH OxidoreductasesPhotochemistryPlant ProteinsProtochlorophyllideStructural Homology, ProteinLight-Harvesting Protein ComplexesNADH, NADPH OxidoreductasesPlant ProteinsProtochlorophyllide

Identifiers

PMID18723681
PMCPMC2527962
OpenAlexW2082171497

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.