Evidence map›Paper›PMID 26416755›Full record

ArticleNature2015

Binding of dinitrogen to an iron-sulfur-carbon site.

Ilija Čorić, Brandon Q Mercado, Eckhard Bill, David J Vinyard, Patrick L Holland

Open access · greenAbstract read
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
6.7field-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

41 citing papers in PubMed, 261 citations in OpenAlex.

  1. Reversible NNational science review · 2026
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  6. Review
  7. Article
  8. Article
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  10. Terminal NChemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Estimations of FeRSC advances · 2022
    Article
  15. Article
  16. Estimations of Fe-NACS omega · 2021
    Article
  17. Partial synthetic models of FeMoco with sulfide and carbyne ligands: Effect of interstitial atom in nitrogenase active site.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Article
  20. Cleavage of cluster iron-sulfide bonds in cyclophane-coordinated FeDalton transactions (Cambridge, England : 2003) · 2021
    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 at 2 institutions in 2 countries.

Ilija ČorićDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, USA.
Brandon Q MercadoDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, USA.
Eckhard BillMax Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
David J VinyardDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, USA.
Patrick L HollandDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, USA.
Yale University · USMax Planck Society · DE

Funding

Low-Coordinate Synthetic Models for Nitrogenase ActivityR01GM065313 · NIGMS · YALE UNIVERSITY · PI PATRICK L HOLLAND · 2004 to 2026
$6.4M
NIGMS NIH HHS GM065313NIGMS NIH HHS R01 GM065313
6 · The paper itself

Abstract

Nitrogenases are the enzymes by which certain microorganisms convert atmospheric dinitrogen (N2) to ammonia, thereby providing essential nitrogen atoms for higher organisms. The most common nitrogenases reduce atmospheric N2 at the FeMo cofactor, a sulfur-rich iron-molybdenum cluster (FeMoco). The central iron sites that are coordinated to sulfur and carbon atoms in FeMoco have been proposed to be the substrate binding sites, on the basis of kinetic and spectroscopic studies. In the resting state, the central iron sites each have bonds to three sulfur atoms and one carbon atom. Addition of electrons to the resting state causes the FeMoco to react with N2, but the geometry and bonding environment of N2-bound species remain unknown. Here we describe a synthetic complex with a sulfur-rich coordination sphere that, upon reduction, breaks an Fe-S bond and binds N2. The product is the first synthetic Fe-N2 complex in which iron has bonds to sulfur and carbon atoms, providing a model for N2 coordination in the FeMoco. Our results demonstrate that breaking an Fe-S bond is a chemically reasonable route to N2 binding in the FeMoco, and show structural and spectroscopic details for weakened N2 on a sulfur-rich iron site.

Indexed as

Binding SitesCarbonElectronsIronLigandsMolybdoferredoxinNitrogenNitrogenaseSulfurCarbonIronLigandsMolybdoferredoxinNitrogenNitrogenaseSulfur

Identifiers

PMID26416755
PMCPMC4592811
OpenAlexW1940696028

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.