Evidence map›Paper›PMID 34545877›Full record

ArticleDalton transactions (Cambridge, England : 2003)2021

Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.

Simone Morra, Jifu Duan, Martin Winkler, Philip A Ash, Thomas Happe, Kylie A Vincent

Open access · hybridAbstract read
In one paragraph

Article in Dalton transactions (Cambridge, England : 2003), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

7 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Crystallise, poise, capture: a multimodal platform for correlated structural and spectroscopic characterisation of redox enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
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  4. Review
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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

6 authors at 2 institutions in 2 countries.

Simone MorraDepartment of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, United Kingdom. kylie.vincent@chem.ox.ac.uk.ORCID http://orcid.org/0000-0003-1341-191X
Jifu DuanFaculty of Biology and Biotechnology, AG Photobiotechnology, Ruhr-University Bochum, 44801 Bochum, Germany.ORCID http://orcid.org/0000-0002-5158-2253
Martin WinklerFaculty of Biology and Biotechnology, AG Photobiotechnology, Ruhr-University Bochum, 44801 Bochum, Germany.
Philip A AshDepartment of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, United Kingdom. kylie.vincent@chem.ox.ac.uk.ORCID http://orcid.org/0000-0001-5264-464X
Thomas HappeFaculty of Biology and Biotechnology, AG Photobiotechnology, Ruhr-University Bochum, 44801 Bochum, Germany.ORCID http://orcid.org/0000-0003-1206-5234
Kylie A VincentDepartment of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, United Kingdom. kylie.vincent@chem.ox.ac.uk.ORCID http://orcid.org/0000-0001-6444-9382
Ruhr University Bochum · DEUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elucidating the distribution of intermediates at the active site of redox metalloenzymes is vital to understanding their highly efficient catalysis. Here we demonstrate that it is possible to generate, and detect, the key catalytic redox states of an [FeFe]-hydrogenase in a protein crystal. Individual crystals of the prototypical [FeFe]-hydrogenase I from

Identifiers

PMID34545877
PMCPMC8453692
OpenAlexW3180190902

What OpenQuestion holds

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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.