Evidence map›Paper›PMID 25184795›Full record

ArticleJournal of the American Chemical Society2014

A 10(6)-fold enhancement in N2-binding affinity of an Fe2(μ-H)2 core upon reduction to a mixed-valence Fe(II)Fe(I) state.

Jonathan Rittle, Charles C L McCrory, Jonas C Peters

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. EPR andInorganic chemistry · 2025
    Article
  2. Review
  3. On the Shoulders of Giants-Reaching for Nitrogenase.Molecules (Basel, Switzerland) · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Spectroscopy of Nitrogenases.Chemical reviews · 2020
    Review
  10. Article
  11. Size-Dependent Association of Cobalt Deuteride Cluster Anions CoJournal of the American Society for Mass Spectrometry · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. ENDOR Characterization of (NInorganic chemistry · 2018
    Article
  16. An S =Journal of the American Chemical Society · 2018
    Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors.

Jonathan RittleDivision of Chemistry and Chemical Engineering, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Charles C L McCrory
Jonas C Peters

Funding

Functional LnFe-Nx Models of Biological N2 FixationR01GM070757 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PETERS, JONAS C · 2005 to 2023
$5.5M
NIGMS NIH HHS GM 070757NIGMS NIH HHS R01 GM070757
6 · The paper itself

Abstract

Transient hydride ligands bridging two or more iron centers purportedly accumulate on the iron-molybdenum cofactor (FeMoco) of nitrogenase, and their role in the reduction of N2 to NH3 is unknown. One role of these ligands may be to facilitate N2 coordination at an iron site of FeMoco. Herein, we consider this hypothesis and describe the preparation of a series of diiron complexes supported by two bridging hydride ligands. These compounds bind either one or two molecules of N2 depending on the redox state of the Fe2(μ-H)2 unit. An unusual example of a mixed-valent Fe(II)(μ-H)2Fe(I) is described that displays a 10(6)-fold enhancement of N2 binding affinity over its oxidized congener, quantified by spectroscopic and electrochemical techniques. Furthermore, these compounds show promise as functional models of nitrogenase as substantial amounts of NH3 are produced upon exposure to proton and electron equivalents. The Fe(μ-H)Fe(N2) sub-structure featured herein was previously unknown. This subunit may be relevant to consider in nitrogenases during turnover.

Indexed as

AmmoniaBinding SitesElectrochemical TechniquesHydrogenIron CompoundsModels, MolecularMolecular StructureMolybdenumNitrogenNitrogenaseOxidation-ReductionAmmoniaHydrogenIron CompoundsMolybdenumNitrogenNitrogenase

Identifiers

PMID25184795
PMCPMC4183624

What OpenQuestion holds

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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.