Evidence map›Paper›PMID 24311779›Full record

ArticleThe Journal of biological chemistry2014

The bidirectional NiFe-hydrogenase in Synechocystis sp. PCC 6803 is reduced by flavodoxin and ferredoxin and is essential under mixotrophic, nitrate-limiting conditions.

Kirstin Gutekunst, Xi Chen, Karoline Schreiber, Ursula Kaspar, Srinivas Makam, Jens Appel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 140 citations in OpenAlex.

  1. Genetic dissection of formate hydrogenlyase-2 function: a metalloenzyme involved in bacterial hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  2. Article
  3. Toward Sustainability: Intensification of Light-Driven Whole Cell Biocatalysis.Chembiochem : a European journal of chemical biology · 2026
    Review
  4. Article
  5. Co-expression of auxiliary genes enhances the activity of a heterologous OBiotechnology for biofuels and bioproducts · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Photobiohydrogen Production and Strategies for HAdvances in biochemical engineering/biotechnology · 2023
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Frontiers in microbiology · 2022
    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

6 authors at 2 institutions in 2 countries.

Kirstin GutekunstFrom the Botanical Institute, Christian-Albrechts-University, 24118 Kiel, Germany and.
Xi Chen
Karoline Schreiber
Ursula Kaspar
Srinivas Makam
Jens Appel
Kiel University · DEArizona State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyanobacteria are able to use solar energy for the production of hydrogen. It is generally accepted that cyanobacterial NiFe-hydrogenases are reduced by NAD(P)H. This is in conflict with thermodynamic considerations, as the midpoint potentials of NAD(P)H do not suffice to support the measured hydrogen production under physiological conditions. We show that flavodoxin and ferredoxin directly reduce the bidirectional NiFe-hydrogenase of Synechocystis sp. PCC 6803 in vitro. A merodiploid ferredoxin-NADP reductase mutant produced correspondingly more photohydrogen. We furthermore found that the hydrogenase receives its electrons via pyruvate:flavodoxin/ferredoxin oxidoreductase (PFOR)-flavodoxin/ferredoxin under fermentative conditions, enabling the cells to gain ATP. These results strongly support that the bidirectional NiFe-hydrogenases in cyanobacteria function as electron sinks for low potential electrons from photosystem I and as a redox balancing device under fermentative conditions. However, the selective advantage of this enzyme is not known. No strong phenotype of mutants lacking the hydrogenase has been found. Because bidirectional hydrogenases are widespread in aquatic nutrient-rich environments that are capable of triggering phytoplankton blooms, we mimicked those conditions by growing cells in the presence of increased amounts of dissolved organic carbon and dissolved organic nitrogen. Under these conditions the hydrogenase was found to be essential. As these conditions close the two most important sinks for reduced flavodoxin/ferredoxin (CO2-fixation and nitrate reduction), this discovery further substantiates the connection between flavodoxin/ferredoxin and the NiFe-hydrogenase.

Indexed as

Bacterial ProteinsFerredoxinsFlavodoxinHydrogenaseNitratesOxidation-ReductionPhotosystem I Protein ComplexSynechocystisBacterial ProteinsFerredoxinsFlavodoxinHydrogenasenickel-iron hydrogenaseNitratesPhotosystem I Protein ComplexBioenergyCyanobacteriaHydrogenasePhotosynthesisPhysiologyRedox

Identifiers

PMID24311779
PMCPMC3900943
OpenAlexW2054267555

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.