Evidence map›Paper›PMID 27607732›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Proton-Coupled Reduction of an Iron Cyanide Complex to Methane and Ammonia.

Jonathan Rittle, Jonas C Peters

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. The Spectroscopy of Nitrogenases.Chemical reviews · 2020
    Review
  8. Article
  9. 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

2 authors at 1 institution in 1 country.

Jonathan RittleDivision of Chemistry and Chemical Engineering, California Institute of Technology, USA.
Jonas C PetersDivision of Chemistry and Chemical Engineering, California Institute of Technology, USA. jpeters@caltech.edu.ORCID 0000-0002-6610-4414
California Institute of Technology · US

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 R01 GM070757
6 · The paper itself

Abstract

Nitrogenase enzymes mediate the six-electron reductive cleavage of cyanide to CH4 and NH3 . Herein we demonstrate for the first time the liberation of CH4 and NH3 from a well-defined iron cyanide coordination complex, [SiP(iPr) 3 ]Fe(CN) (where [SiP(iPr) 3 ] represents a tris(phosphine)silyl ligand), on exposure to proton and electron equivalents. [SiP(iPr) 3 ]Fe(CN) additionally serves as a useful entry point to rare examples of terminally-bound Fe(CNH) and Fe(CNH2 ) species that, in accord with preliminary mechanistic studies, are plausible intermediates of the cyanide reductive protonation to generate CH4 and NH3 . Comparative studies with a related [SiP(iPr) 3 ]Fe(CNMe2 ) complex suggests the possibility of multiple, competing mechanisms for cyanide activation and reduction.

Indexed as

AmmoniaCatalysisCoordination ComplexesCrystallography, X-RayCyanidesIronLigandsMethaneMolecular ConformationOxidation-ReductionProtonsAmmoniaCoordination ComplexesCyanidesIronLigandsMethaneProtonscarbyne ligandscyanide cleavageiron complexesnitrogenasenitrogen fixation

Identifiers

PMID27607732
PMCPMC5065330
OpenAlexW2517614490

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.