Evidence map›Paper›PMID 23934246›Full record

ArticleNature chemical biology2013

Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic.

Julian Esselborn, Camilla Lambertz, Agnieszka Adamska-Venkates, Trevor Simmons, Gustav Berggren, Jens Noth, Judith Siebel, Anja Hemschemeier, Vincent Artero, Edward Reijerse and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
14.2field-weighted citation impact, top 1% 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

119 citing papers in PubMed, 346 citations in OpenAlex.

  1. Synthesis of diiron subcluster [FeNature protocols · 2026
    Review
  2. Biosynthesis of the Selenium-Substituted [FeFe]-Hydrogenases.Journal of the American Chemical Society · 2026
    Article
  3. Article
  4. Subunit fusion unlocks rapidChemical science · 2026
    Article
  5. Article
  6. Article
  7. [FeFe] hydrogenases with modified azadithiolate bridgeheads serve as unidirectional hydrogen oxidation catalysts.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  8. Article
  9. Article
  10. Turning the FeFe hydrogenase fromProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  12. Review
  13. Distinct Valence States of the [4Fe4S] Cluster Revealed in the Hydrogenase CrHydA1.Angewandte Chemie (International ed. in English) · 2025
    Article
  14. A [FeFe] Hydrogenase-Rubrerythrin Chimeric Enzyme Functions to Couple HJournal of the American Chemical Society · 2025
    Article
  15. Article
  16. Structural determinants of oxygen resistance and ZnProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Synthesis of [FeOrganometallics · 2025
    Article
  18. Article
  19. Final Stages in the Biosynthesis of the [FeFe]-Hydrogenase Active Site.Angewandte Chemie (International ed. in English) · 2024
    Article
  20. Outer-sphere effects on the OChemical science · 2024
    Review

59 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 3 countries.

Julian EsselbornRuhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, 44801 Bochum, Germany.
Camilla Lambertz *Ruhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, 44801 Bochum, Germany.
Agnieszka Adamska-Venkates *Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
Trevor Simmons *Laboratoire de Chimie et Biologie des Métaux (CEA / Université Grenoble 1 / CNRS), 17 rue des Martyrs, F-38054 Grenoble cedex 9, France.
Gustav BerggrenLaboratoire de Chimie et Biologie des Métaux (CEA / Université Grenoble 1 / CNRS), 17 rue des Martyrs, F-38054 Grenoble cedex 9, France.
Jens NothRuhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, 44801 Bochum, Germany.
Judith SiebelMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
Anja HemschemeierRuhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, 44801 Bochum, Germany.
Vincent ArteroLaboratoire de Chimie et Biologie des Métaux (CEA / Université Grenoble 1 / CNRS), 17 rue des Martyrs, F-38054 Grenoble cedex 9, France.
Edward ReijerseMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
Marc FontecaveLaboratoire de Chimie et Biologie des Métaux (CEA / Université Grenoble 1 / CNRS), 17 rue des Martyrs, F-38054 Grenoble cedex 9, France.
Wolfgang LubitzMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
Thomas HappeRuhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, 44801 Bochum, Germany.
Ruhr University Bochum · DEMax Planck Institute for Chemical Energy Conversion · DELaboratoire de Chimie et Biologie des Métaux · FRCollège de France · FRUniversité Grenoble Alpes · FR

Funding

European Research Council 306398
6 · The paper itself

Abstract

Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H₂-producing catalysts.

Indexed as

ApoenzymesBiocatalysisCatalytic DomainCoenzymesEnzyme ActivationHydrogenHydrogenaseIronIron-Sulfur ProteinsModels, MolecularApoenzymesCoenzymesHydrogenHydrogenaseIroniron hydrogenaseIron-Sulfur Proteins

Identifiers

PMID23934246
PMCPMC3795299
OpenAlexW2012073519

What OpenQuestion holds

Textmetadata
LicenceTDM
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.