Evidence map›Paper›PMID 26580976›Full record

ArticlePloS one2015

Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase.

Nina Heidary, Tillmann Utesch, Maximilian Zerball, Marius Horch, Diego Millo, Johannes Fritsch, Oliver Lenz, Regine von Klitzing, Peter Hildebrandt, Anna Fischer and 2 more

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Stepwise conversion of the CysChemical science · 2023
    Article
  2. Enzyme immobilization studied through molecular dynamic simulations.Frontiers in bioengineering and biotechnology · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. A L-proline/OMolecular biology reports · 2018
    Article
  10. 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

12 authors.

Nina HeidaryInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Tillmann UteschInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Maximilian ZerballInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Marius HorchInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Diego MilloBiomolecular Spectroscopy/LaserLaB Amsterdam, Vrije Universiteit Amsterdam, De Boelelaan 1083, NL-1081 HV Amsterdam, The Netherlands.
Johannes FritschInstitut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Chausseestraße 117, D-10115, Berlin, Germany.
Oliver LenzInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Regine von KlitzingInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Peter HildebrandtInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Anna FischerInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Maria Andrea MroginskiInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.
Ingo ZebgerInstitut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135 & 124, D-10623, Berlin, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein immobilization on electrodes is a key concept in exploiting enzymatic processes for bioelectronic devices. For optimum performance, an in-depth understanding of the enzyme-surface interactions is required. Here, we introduce an integral approach of experimental and theoretical methods that provides detailed insights into the adsorption of an oxygen-tolerant [NiFe] hydrogenase on a biocompatible gold electrode. Using atomic force microscopy, ellipsometry, surface-enhanced IR spectroscopy, and protein film voltammetry, we explore enzyme coverage, integrity, and activity, thereby probing both structure and catalytic H2 conversion of the enzyme. Electrocatalytic efficiencies can be correlated with the mode of protein adsorption on the electrode as estimated theoretically by molecular dynamics simulations. Our results reveal that pre-activation at low potentials results in increased current densities, which can be rationalized in terms of a potential-induced re-orientation of the immobilized enzyme.

Indexed as

BiocatalysisAdsorptionElectrochemistryElectrodesEnzymes, ImmobilizedEnzyme StabilityHydrogenaseMolecular Dynamics SimulationNanostructuresOxygenRalstoniaSpectrophotometry, InfraredEnzymes, ImmobilizedHydrogenasenickel-iron hydrogenaseOxygen

Identifiers

PMID26580976
PMCPMC4651547

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.