Evidence map›Paper›PMID 27768098›Full record

ArticleNature chemistry2016

Nickel-centred proton reduction catalysis in a model of [NiFe] hydrogenase.

Deborah Brazzolotto, Marcello Gennari, Nicolas Queyriaux, Trevor R Simmons, Jacques Pécaut, Serhiy Demeshko, Franc Meyer, Maylis Orio, Vincent Artero, Carole Duboc

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 240 citations in OpenAlex.

  1. Article
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  12. Development of (NO)Fe(NAccounts of chemical research · 2024
    Article
  13. Article
  14. Review
  15. Electro- and photochemical HSustainable energy & fuels · 2023
    Article
  16. Hybrids of [FeFe]- and [NiFe]-HOrganometallics · 2023
    Article
  17. Enzymatic and Bioinspired Systems for Hydrogen Production.International journal of molecular sciences · 2023
    Review
  18. Article
  19. Article
  20. 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 at 7 institutions in 5 countries.

Deborah BrazzolottoUniv. Grenoble Alpes, CNRS UMR 5250, DCM, F-38000 Grenoble, France.
Marcello GennariUniv. Grenoble Alpes, CNRS UMR 5250, DCM, F-38000 Grenoble, France.
Nicolas QueyriauxUniv. Grenoble Alpes, CNRS UMR 5249, CEA, Laboratoire de Chimie et Biologie des Métaux, F-38000 Grenoble, France.
Trevor R SimmonsUniv. Grenoble Alpes, CNRS UMR 5249, CEA, Laboratoire de Chimie et Biologie des Métaux, F-38000 Grenoble, France.
Jacques PécautUniv. Grenoble Alpes, INAC-LCIB, F-38000 Grenoble, France.
Serhiy DemeshkoInstitute of Inorganic Chemistry, Georg-August-University Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany.
Franc MeyerInstitute of Inorganic Chemistry, Georg-August-University Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany.
Maylis OrioInstitut des Sciences Moléculaires de Marseille, Aix Marseille Université, CNRS, Centrale Marseille, ISM2 UMR 7313, 13397, Marseille, France.
Vincent ArteroUniv. Grenoble Alpes, CNRS UMR 5249, CEA, Laboratoire de Chimie et Biologie des Métaux, F-38000 Grenoble, France.
Carole DubocUniv. Grenoble Alpes, CNRS UMR 5250, DCM, F-38000 Grenoble, France.
Laboratoire de Chimie et Biologie des Métaux · FRInstitute of Inorganic Chemistry of the Slovak Academy of Sciences · SKCentrale Marseille · FRDépartement de Chimie Moléculaire · FRLaboratoire de Chimie de Coordination · FRUniversité Grenoble Alpes · FRUniversity of East Anglia · GB

Funding

European Research Council 306398
6 · The paper itself

Abstract

Hydrogen production through water splitting is one of the most promising solutions for the storage of renewable energy. [NiFe] hydrogenases are organometallic enzymes containing nickel and iron centres that catalyse hydrogen evolution with performances that rival those of platinum. These enzymes provide inspiration for the design of new molecular catalysts that do not require precious metals. However, all heterodinuclear NiFe models reported so far do not reproduce the Ni-centred reactivity found at the active site of [NiFe] hydrogenases. Here, we report a structural and functional NiFe mimic that displays reactivity at the Ni site. This is shown by the detection of two catalytic intermediates that reproduce structural and electronic features of the Ni-L and Ni-R states of the enzyme during catalytic turnover. Under electrocatalytic conditions, this mimic displays high rates for H

Indexed as

Biomimetic MaterialsCatalysisCatalytic DomainCoordination ComplexesCrystallography, X-RayElectron Spin Resonance SpectroscopyHydrogenHydrogenaseModels, MolecularMolecular ConformationNickelOxidation-ReductionProtonsCoordination ComplexesHydrogenHydrogenaseNickelnickel-iron hydrogenaseProtons

Identifiers

PMID27768098
PMCPMC5493981
OpenAlexW2488311164

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.