Evidence map›Paper›PMID 25143219›Full record

ArticleNature chemistry2014

A redox hydrogel protects hydrogenase from high-potential deactivation and oxygen damage.

Nicolas Plumeré, Olaf Rüdiger, Alaa Alsheikh Oughli, Rhodri Williams, Jeevanthi Vivekananthan, Sascha Pöller, Wolfgang Schuhmann, Wolfgang Lubitz

Abstract 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. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

  1. Article
  2. Review
  3. Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026
    Review
  4. Review
  5. Article
  6. Surface Immobilization of Metalloenzymes Usinga Pyrene-Modified Hydrogel.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Cobaltocene Polymers for Low-Potential Enzymatic Electrocatalysis.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  8. Turning the FeFe hydrogenase fromProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Connecting Biological and Synthetic Approaches for Electrocatalytic COAngewandte Chemie (International ed. in English) · 2024
    Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Stability of the H-cluster under whole-cell conditions-formation of an HJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
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

8 authors.

Nicolas Plumeré1] Center for Electrochemical Sciences-Molecular Nanostructures, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany [2].
Olaf Rüdiger1] Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany [2].
Alaa Alsheikh Oughli1] Center for Electrochemical Sciences-Molecular Nanostructures, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany [2] Center for Electrochemical Sciences-Elektroanalytik &Sensorik, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany.
Rhodri WilliamsCenter for Electrochemical Sciences-Molecular Nanostructures, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany.
Jeevanthi VivekananthanCenter for Electrochemical Sciences-Elektroanalytik &Sensorik, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany.
Sascha PöllerCenter for Electrochemical Sciences-Elektroanalytik &Sensorik, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany.
Wolfgang SchuhmannCenter for Electrochemical Sciences-Elektroanalytik &Sensorik, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany.ORCID 0000000329165223
Wolfgang LubitzMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrogenases are nature's efficient catalysts for both the generation of energy via oxidation of molecular hydrogen and the production of hydrogen via the reduction of protons. However, their O2 sensitivity and deactivation at high potential limit their applications in practical devices, such as fuel cells. Here, we show that the integration of an O2-sensitive hydrogenase into a specifically designed viologen-based redox polymer protects the enzyme from O2 damage and high-potential deactivation. Electron transfer between the polymer-bound viologen moieties controls the potential applied to the active site of the hydrogenase and thus insulates the enzyme from excessive oxidative stress. Under catalytic turnover, electrons provided from the hydrogen oxidation reaction induce viologen-catalysed O2 reduction at the polymer surface, thus providing self-activated protection from O2. The advantages of this tandem protection are demonstrated using a single-compartment biofuel cell based on an O2-sensitive hydrogenase and H2/O2 mixed feed under anode-limiting conditions.

Indexed as

Binding SitesBioelectric Energy SourcesElectron TransportHydrogel, Polyethylene Glycol DimethacrylateHydrogenaseOxidation-ReductionOxygenViologensHydrogel, Polyethylene Glycol DimethacrylateHydrogenaseOxygenViologens

Identifiers

PMID25143219

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.