Evidence map›Paper›PMID 24678667›Full record

ReviewCurrent protein & peptide science2014

The end of the line: can ferredoxin and ferredoxin NADP(H) oxidoreductase determine the fate of photosynthetic electrons?

Tatjana Goss, Guy Hanke

Open access · bronzeAbstract readReview
In one paragraph

Review in Current protein & peptide science, 2014. 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
2.8field-weighted citation impact, top 9% 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, 71 citations in OpenAlex.

  1. Structural proteomics reveals the functional docking interface of ferredoxin-NADPThe Plant journal : for cell and molecular biology · 2026
    Article
  2. Article
  3. Review
  4. Optimising COMicrobial cell factories · 2025
    Article
  5. Confocal Laser Scanning Microscopy of Light-Independent ROS inInternational journal of molecular sciences · 2025
    Article
  6. Article
  7. Redox-dependent hydrogen-bond network rearrangement of ferredoxin-NADPActa crystallographica. Section F, Structural biology communications · 2025
    Article
  8. Review
  9. Thylakoid Rhodanese-like Protein-Ferredoxin:NADPAntioxidants (Basel, Switzerland) · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Upregulation of bundle sheath electron transport capacity under limiting light in CThe Plant journal : for cell and molecular biology · 2021
    Article
  17. Review
  18. Article
  19. Developmental acclimation of the thylakoid proteome to light intensity in Arabidopsis.The Plant journal : for cell and molecular biology · 2021
    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

2 authors at 1 institution in 1 country.

Tatjana Goss
Guy HankeDepartment of Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück,11 Barbara Strasse, Osnabrueck, DE-49076, Germany. guy.hanke@biologie.uni-osnabrueck.de.
Osnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

At the end of the linear photosynthetic electron transfer (PET) chain, the small soluble protein ferredoxin (Fd) transfers electrons to Fd:NADP(H) oxidoreductase (FNR), which can then reduce NADP+ to support C assimilation. In addition to this linear electron flow (LEF), Fd is also thought to mediate electron flow back to the membrane complexes by different cyclic electron flow (CEF) pathways: either antimycin A sensitive, NAD(P)H complex dependent, or through FNR located at the cytochrome b6f complex. Both Fd and FNR are present in higher plant genomes as multiple gene copies, and it is now known that specific Fd iso-proteins can promote CEF. In addition, FNR iso-proteins vary in their ability to dynamically interact with thylakoid membrane complexes, and it has been suggested that this may also play a role in CEF. We will highlight work on the different Fd-isoproteins and FNR-membrane association found in the bundle sheath (BSC) and mesophyll (MC) cell chloroplasts of the C4 plant maize. These two cell types perform predominantly CEF and LEF, and the properties and activities of Fd and FNR in the BSC and MC are therefore specialized for CEF and LEF respectively. A diversity of Fd isoproteins and dynamic FNR location has also been recorded in C3 plants, algae and cyanobacteria. This indicates that the principles learned from the extreme electron transport situations in the BSC and MC of maize might be usefully applied to understanding the dynamic transition between these states in other systems.

Indexed as

ElectronsPhotosynthesisFerredoxin-NADP ReductaseFerredoxinsFerredoxin-NADP ReductaseFerredoxins

Identifiers

PMID24678667
PMCPMC4030315
OpenAlexW1991463968

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.