Evidence map›Paper›PMID 39544119›Full record

ArticleChembiochem : a European journal of chemical biology2025

Understanding the P-Cluster of Vanadium Nitrogenase: an EPR and XAS Study of the Holo vs. Apo Forms of the Enzyme.

Isis M Wahl, Kushal Sengupta, Maurice van Gastel, Laure Decamps, Serena DeBeer

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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

5 authors.

Isis M WahlDepartment of Inorganic Spectroscopy, Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, Mülheim an der Ruhr, 45470, Germany.ORCID https://orcid.org/0000-0001-5074-7493
Kushal SenguptaDepartment of Inorganic Spectroscopy, Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, Mülheim an der Ruhr, 45470, Germany.ORCID https://orcid.org/0000-0002-5941-406X
Maurice van GastelDepartment of Molecular Theory and Spectroscopy, Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhem-Platz 1, Mülheim an der Ruhr, 45470, Germany.ORCID https://orcid.org/0000-0002-1547-6365
Laure DecampsDepartment of Inorganic Spectroscopy, Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, Mülheim an der Ruhr, 45470, Germany.ORCID https://orcid.org/0000-0002-4572-7479
Serena DeBeerDepartment of Inorganic Spectroscopy, Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, Mülheim an der Ruhr, 45470, Germany.ORCID https://orcid.org/0000-0002-5196-3400

Funding

Alexander von Humboldt-StiftungMax-Planck-Gesellschaft
6 · The paper itself

Abstract

The catalytic moiety of nitrogenases contains two complex metalloclusters: The M-cluster (also called cofactor), where the catalytic reduction of substrates takes place, and the [Fe

Indexed as

NitrogenaseVanadiumApoenzymesElectron Spin Resonance SpectroscopyHoloenzymesOxidation-ReductionX-Ray Absorption SpectroscopyApoenzymesHoloenzymesNitrogenaseVanadiumEPREXAFSFeS clusterNitrogenaseP-clusterXAS

Identifiers

PMID39544119
PMCPMC11823357

What OpenQuestion holds

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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.