Evidence map›Paper›PMID 24100040›Full record

ArticleThe Journal of biological chemistry2013

Identification of global ferredoxin interaction networks in Chlamydomonas reinhardtii.

Erin A Peden, Marko Boehm, David W Mulder, Reanna Davis, William M Old, Paul W King, Maria L Ghirardi, Alexandra Dubini

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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed, 108 citations in OpenAlex.

  1. Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  2. Light-Driven HPlants (Basel, Switzerland) · 2024
    Review
  3. Article
  4. The AlgaInternational journal of molecular sciences · 2023
    Article
  5. Changing the tracks: screening for electron transfer proteins to support hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  6. Article
  7. Article
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  10. The Chloroplast ofInternational journal of molecular sciences · 2021
    Review
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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

8 authors at 2 institutions in 1 country.

Erin A PedenFrom the National Renewable Energy Laboratory, Golden, Colorado 80401 and.
Marko Boehm
David W Mulder
Reanna Davis
William M Old
Paul W King
Maria L Ghirardi
Alexandra Dubini
National Renewable Energy Laboratory · USUniversity of Colorado Boulder · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ferredoxins (FDXs) can distribute electrons originating from photosynthetic water oxidation, fermentation, and other reductant-generating pathways to specific redox enzymes in different organisms. The six FDXs identified in Chlamydomonas reinhardtii are not fully characterized in terms of their biological function. In this report, we present data from the following: (a) yeast two-hybrid screens, identifying interaction partners for each Chlamydomonas FDX; (b) pairwise yeast two-hybrid assays measuring FDX interactions with proteins from selected biochemical pathways; (c) affinity pulldown assays that, in some cases, confirm and even expand the interaction network for FDX1 and FDX2; and (d) in vitro NADP(+) reduction and H2 photo-production assays mediated by each FDX that verify their role in these two pathways. Our results demonstrate new potential roles for FDX1 in redox metabolism and carbohydrate and fatty acid biosynthesis, for FDX2 in anaerobic metabolism, and possibly in state transition. Our data also suggest that FDX3 is involved in nitrogen assimilation, FDX4 in glycolysis and response to reactive oxygen species, and FDX5 in hydrogenase maturation. Finally, we provide experimental evidence that FDX1 serves as the primary electron donor to two important biological pathways, NADPH and H2 photo-production, whereas FDX2 is capable of driving these reactions at less than half the rate observed for FDX1.

Indexed as

Algal ProteinsChlamydomonas reinhardtiiFerredoxinsHydrogenaseModels, BiologicalNADPOxidation-ReductionProtein Interaction MapsProtein IsoformsRecombinant ProteinsTwo-Hybrid System TechniquesAlgal ProteinsFerredoxinsHydrogenaseNADPProtein IsoformsRecombinant ProteinsBioenergetics/Electron Transfer ComplexChlamydomonasEnergy MetabolismFerredoxinNetworkProtein-Protein InteractionsRedox

Identifiers

PMID24100040
PMCPMC3853270
OpenAlexW2010244877

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.