Evidence map›Paper›PMID 24651202›Full record

ArticleNature chemistry2014

The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster.

Vincent Fourmond, Claudio Greco, Kateryna Sybirna, Carole Baffert, Po-Hung Wang, Pierre Ezanno, Marco Montefiori, Maurizio Bruschi, Isabelle Meynial-Salles, Philippe Soucaille and 4 more

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer.Journal of the American Chemical Society · 2019
    Article
  10. The final steps of [FeFe]-hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Article
  13. Mechanism of ONature chemistry · 2017
    Article
  14. Article
  15. Stepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Vincent FourmondAix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.
Claudio GrecoDepartment of Earth and Environmental Science, Università degli Studi di Milano-Bicocca, P.zza della Scienza 1, Milan 20126, Italy.
Kateryna SybirnaiBiTec-S, SB2SM, LMB (UMR CNRS 8221), DSV, CEA, 91191 Gif-sur-Yvette, France.
Carole BaffertAix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.
Po-Hung WangUniversity College London, Department of Physics and Astronomy, Gower Street, London WC1E 6BT, UK.
Pierre EzannoAix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.
Marco MontefioriUniversity College London, Department of Physics and Astronomy, Gower Street, London WC1E 6BT, UK.
Maurizio BruschiDepartment of Earth and Environmental Science, Università degli Studi di Milano-Bicocca, P.zza della Scienza 1, Milan 20126, Italy.
Isabelle Meynial-SallesUniversité de Toulouse, INSA, UPS, INP, LISBP, INRA:UMR792,135 CNRS:UMR 5504, avenue de Rangueil, 31077 Toulouse, France.
Philippe SoucailleUniversité de Toulouse, INSA, UPS, INP, LISBP, INRA:UMR792,135 CNRS:UMR 5504, avenue de Rangueil, 31077 Toulouse, France.
Jochen BlumbergerUniversity College London, Department of Physics and Astronomy, Gower Street, London WC1E 6BT, UK.
Hervé BottiniBiTec-S, SB2SM, LMB (UMR CNRS 8221), DSV, CEA, 91191 Gif-sur-Yvette, France.
Luca De GioiaDepartment of Biotechnology and Biosciences, Università degli Studi di Milano-Bicocca, P.zza della Scienza 2, Milan 20126, Italy.
Christophe LégerAix Marseille Université, CNRS, BIP UMR 7281, 13402, Marseille, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nature is a valuable source of inspiration in the design of catalysts, and various approaches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H2. In FeFe hydrogenases, H2 oxidation occurs at the H-cluster, and catalysis involves H2 binding on the vacant coordination site of an iron centre. Here, we show that the reversible oxidative inactivation of this enzyme results from the binding of H2 to coordination positions that are normally blocked by intrinsic CO ligands. This flexibility of the coordination sphere around the reactive iron centre confers on the enzyme the ability to avoid harmful reactions under oxidizing conditions, including exposure to O2. The versatile chemistry of the diiron cluster in the natural system might inspire the design of novel synthetic catalysts for H2 oxidation.

Indexed as

HydrogenHydrogenaseIron-Sulfur ProteinsKineticsMutationOxidation-ReductionPhenylalanineProtein ConformationTyrosineHydrogenHydrogenaseiron hydrogenaseIron-Sulfur ProteinsPhenylalanineTyrosine

Identifiers

PMID24651202

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.