Evidence map›Paper›PMID 39699648›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2025

The nitrogenase mechanism: new roles for the dangler?

Rebeccah A Warmack, Douglas C Rees

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Magnetic interactions between metal sites in complex enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    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

2 authors.

Rebeccah A WarmackDivision of Chemistry and Chemical Engineering, California Institute of Technology, 164-30, Pasadena, CA, 91125, USA.
Douglas C ReesDivision of Chemistry and Chemical Engineering, Howard Hughes Medical Institute, California Institute of Technology, 147-75, Pasadena, CA, 91125, USA. dcrees@caltech.edu.

Funding

In situ mechanisms of biological nitrogen fixationK99GM152765 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI WARMACK, REBECCAH · 2024 to 2025
$247k
Atomic Models of Nitrogen Fixation by Nitrogenase from CryoEM StructuresF32GM143836 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI WARMACK, REBECCAH · 2021 to 2022
$136k
NIGMS NIH HHS F32 GM143836NIGMS NIH HHS K99 GM152765NIH HHS GM143836
6 · The paper itself

Abstract

Dangler sites protruding from a core metallocluster were introduced into the bioinorganic lexicon in 2000 by R.D. Britt and co-workers in an analysis of the tetramanganese oxygen-evolving cluster in photosystem II. In this perspective, we consider whether analogous dangler sites could participate in the mechanism of dinitrogen reduction by nitrogenase. Two possible roles for dynamic danglers in the active site FeMo cofactor are highlighted that might occur transiently during turnover. The first role for a dangler involves the S2B belt sulfur associated with displacement by carbon monoxide and other ligands, while the second dangler role could involve the entire cluster upon displacement of the His-

Indexed as

NitrogenaseCatalytic DomainModels, MolecularMolybdenumMolybdoferredoxinMolybdenumMolybdoferredoxinNitrogenaseIron–sulfur clustersMetalloproteinsNitrogenaseNitrogen fixation

Identifiers

PMID39699648
PMCPMC11928389

What OpenQuestion holds

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Registered trials

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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.