Evidence map›Paper›PMID 19846550›Full record

ArticleThe Journal of biological chemistry2009

Characterization of the key step for light-driven hydrogen evolution in green algae.

Martin Winkler, Sebastian Kuhlgert, Michael Hippler, Thomas Happe

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.5field-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

32 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  4. Light-Driven HPlants (Basel, Switzerland) · 2024
    Review
  5. The AlgaInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. 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
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Frequency and potential dependence of reversible electrocatalytic hydrogen interconversion by [FeFe]-hydrogenases.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
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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

4 authors at 2 institutions in 1 country.

Martin WinklerLehrstuhl Biochemie der Pflanzen, AG Photobiotechnologie, Ruhr-Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany.
Sebastian KuhlgertInstitut für Biochemie und Biotechnologie der Pflanzen, Universität Münster, Hindenburgplatz 55, 49143 Münster, Germany.
Michael HipplerInstitut für Biochemie und Biotechnologie der Pflanzen, Universität Münster, Hindenburgplatz 55, 49143 Münster, Germany.
Thomas HappeLehrstuhl Biochemie der Pflanzen, AG Photobiotechnologie, Ruhr-Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany. Electronic address: thomas.happe@rub.de.
Ruhr University Bochum · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Under anaerobic conditions, several species of green algae perform a light-dependent hydrogen production catalyzed by a special group of [FeFe] hydrogenases termed HydA. Although highly interesting for biotechnological applications, the direct connection between photosynthetic electron transport and hydrogenase activity is still a matter of speculation. By establishing an in vitro reconstitution system, we demonstrate that the photosynthetic ferredoxin (PetF) is essential for efficient electron transfer between photosystem I and HydA1. To investigate the electrostatic interaction process and electron transfer between PetF and HydA1, we performed site-directed mutagenesis. Kinetic analyses with several site-directed mutagenesis variants of HydA1 and PetF enabled us to localize the respective contact sites. These experiments in combination with in silico docking analyses indicate that electrostatic interactions between the conserved HydA1 residue Lys(396) and the C terminus of PetF as well as between the PetF residue Glu(122) and the N-terminal amino group of HydA1 play a major role in complex formation and electron transfer. Mapping of relevant HydA1 and PetF residues constitutes an important basis for manipulating the physiological photosynthetic electron flow in favor of light-driven H(2) production.

Indexed as

Algal ProteinsAnaerobiosisAnimalsChlamydomonas reinhardtiiElectron TransportFerredoxinsHydrogenHydrogenaseLightPeptide MappingPhotosynthesisProtozoan ProteinsAlgal ProteinsFerredoxinsHydrogenHydrogenaseProtozoan Proteins

Identifiers

PMID19846550
PMCPMC2794776
OpenAlexW1999595265

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.