Evidence map›Paper›PMID 30413719›Full record

ArticleNature communications2018

Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases.

Jifu Duan, Moritz Senger, Julian Esselborn, Vera Engelbrecht, Florian Wittkamp, Ulf-Peter Apfel, Eckhard Hofmann, Sven T Stripp, Thomas Happe, Martin Winkler

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Redox regulation in OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  2. Proton Transport as a Missing Design Variable in Immobilized Enzyme Catalysis.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Electrochemical characterization of C. pasteurianum hydrogenase II and three site-directed variants: catalysis and inhibition.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. [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
  9. Article
  10. Article
  11. 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. Article
  15. Structural determinants of oxygen resistance and ZnProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Outer-sphere effects on the OChemical science · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. A personal account on 25 years of scientific literature on [FeFe]-hydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    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

10 authors.

Jifu DuanDepartment of Plant Biochemistry, Photobiotechnology, Ruhr-Universität Bochum, 44801, Bochum, Germany.ORCID http://orcid.org/0000-0002-5158-2253
Moritz SengerDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, 14195, Berlin, Germany.
Julian EsselbornDepartment of Plant Biochemistry, Photobiotechnology, Ruhr-Universität Bochum, 44801, Bochum, Germany.
Vera EngelbrechtDepartment of Plant Biochemistry, Photobiotechnology, Ruhr-Universität Bochum, 44801, Bochum, Germany.
Florian WittkampDepartment of Chemistry and Biochemistry, Inorganic Chemistry Ι, Ruhr-Universität Bochum, 44801, Bochum, Germany.
Ulf-Peter ApfelDepartment of Chemistry and Biochemistry, Inorganic Chemistry Ι, Ruhr-Universität Bochum, 44801, Bochum, Germany.
Eckhard HofmannDepartment of Biophysics, Protein Crystallography, Ruhr-Universität Bochum, 44801, Bochum, Germany.ORCID http://orcid.org/0000-0003-4874-372X
Sven T StrippDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, 14195, Berlin, Germany.ORCID http://orcid.org/0000-0002-8412-0258
Thomas HappeDepartment of Plant Biochemistry, Photobiotechnology, Ruhr-Universität Bochum, 44801, Bochum, Germany. thomas.happe@rub.de.
Martin WinklerDepartment of Plant Biochemistry, Photobiotechnology, Ruhr-Universität Bochum, 44801, Bochum, Germany. martin.winkler-2@rub.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unmatched catalytic turnover rates of [FeFe]-hydrogenases require an exceptionally efficient proton-transfer (PT) pathway to shuttle protons as substrates or products between bulk water and catalytic center. For clostridial [FeFe]-hydrogenase CpI such a pathway has been proposed and analyzed, but mainly on a theoretical basis. Here, eleven enzyme variants of two different [FeFe]-hydrogenases (CpI and HydA1) with substitutions in the presumptive PT-pathway are examined kinetically, spectroscopically, and crystallographically to provide solid experimental proof for its role in hydrogen-turnover. Targeting key residues of the PT-pathway by site directed mutagenesis significantly alters the pH-activity profile of these variants and in presence of H

Indexed as

ProtonsCrystallography, X-RayHydrogenHydrogenaseHydrogen BondingHydrogen-Ion ConcentrationIron-Sulfur ProteinsMutagenesis, Site-DirectedMutant ProteinsSpectrophotometry, InfraredHydrogenHydrogenaseiron hydrogenaseIron-Sulfur ProteinsMutant ProteinsProtons

Identifiers

PMID30413719
PMCPMC6226526

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Registered trials

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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.