Evidence map›Paper›PMID 21606330›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitro.

Iftach Yacoby, Sergii Pochekailov, Hila Toporik, Maria L Ghirardi, Paul W King, Shuguang Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 186 citations in OpenAlex.

  1. Article
  2. Structural proteomics reveals the functional docking interface of ferredoxin-NADPThe Plant journal : for cell and molecular biology · 2026
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  7. Light-Driven HPlants (Basel, Switzerland) · 2024
    Review
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  16. Improved photosynthetic capacity and photosystem I oxidation via heterologous metabolism engineering in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

6 authors at 3 institutions in 2 countries.

Iftach YacobyCenter for Biomedical Engineering NE47-379, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139-4307, USA.
Sergii Pochekailov
Hila Toporik
Maria L Ghirardi
Paul W King
Shuguang Zhang
Massachusetts Institute of Technology · USNational Renewable Energy Laboratory · USTel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic water splitting, coupled to hydrogenase-catalyzed hydrogen production, is considered a promising clean, renewable source of energy. It is widely accepted that the oxygen sensitivity of hydrogen production, combined with competition between hydrogenases and NADPH-dependent carbon dioxide fixation are the main limitations for its commercialization. Here we provide evidence that, under the anaerobic conditions that support hydrogen production, there is a significant loss of photosynthetic electrons toward NADPH production in vitro. To elucidate the basis for competition, we bioengineered a ferredoxin-hydrogenase fusion and characterized hydrogen production kinetics in the presence of Fd, ferredoxin:NADP(+)-oxidoreductase (FNR), and NADP(+). Replacing the hydrogenase with a ferredoxin-hydrogenase fusion switched the bias of electron transfer from FNR to hydrogenase and resulted in an increased rate of hydrogen photoproduction. These results suggest a new direction for improvement of biohydrogen production and a means to further resolve the mechanisms that control partitioning of photosynthetic electron transport.

Indexed as

AlgorithmsAmino Acid SequenceChlamydomonas reinhardtiiElectron TransportFerredoxin-NADP ReductaseFerredoxinsHydrogenHydrogenaseIron-Sulfur ProteinsKineticsLightModels, BiologicalNADPPhotosynthesisPhotosystem I Protein ComplexPlant ProteinsFerredoxin-NADP ReductaseFerredoxinsHydrogenHydrogenaseiron hydrogenaseIron-Sulfur ProteinsNADPPhotosystem I Protein ComplexPlant ProteinsRecombinant Fusion Proteins

Identifiers

PMID21606330
PMCPMC3111258
OpenAlexW2145147173

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.