Evidence map›Paper›PMID 21207999›Full record

ArticleJournal of the American Chemical Society2011

Influence of thiolate ligands on reductive N-O bond activation. Probing the O2(-) binding site of a biomimetic superoxide reductase analogue and examining the proton-dependent reduction of nitrite.

Gloria Villar-Acevedo, Elaine Nam, Sarah Fitch, Jason Benedict, John Freudenthal, Werner Kaminsky, Julie A Kovacs

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 43 citations in OpenAlex.

  1. Unveiling an {FeNO}Journal of the American Chemical Society · 2026
    Article
  2. Article
  3. A Nonheme Mononuclear {FeNO}Angewandte Chemie (International ed. in English) · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Formation of a Reactive, Alkyl Thiolate-Ligated FeJournal of the American Chemical Society · 2019
    Article
  8. Article
  9. Metal-Assisted Oxo Atom Addition to an Fe(III) Thiolate.Journal of the American Chemical Society · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

7 authors at 1 institution in 1 country.

Gloria Villar-Acevedo
Elaine Nam
Sarah Fitch
Jason Benedict
John Freudenthal
Werner Kaminsky
Julie A Kovacs
University of Washington · US

Funding

STRUCTURES INFLUENCE ON REACTIVITY IN METALLOENZYMESR01GM045881 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOVACS, JULIA A · 1992 to 2015
$4.3M
NIGMS NIH HHS GM 45881NIGMS NIH HHS R01 GM045881
6 · The paper itself

Abstract

Nitric oxide (NO) is frequently used to probe the substrate-binding site of "spectroscopically silent" non-heme Fe(2+) sites of metalloenzymes, such as superoxide reductase (SOR). Herein we use NO to probe the superoxide binding site of our thiolate-ligated biomimetic SOR model [Fe(II)(S(Me(2))N(4)(tren))](+) (1). Like NO-bound trans-cysteinate-ligated SOR (SOR-NO), the rhombic S = 3/2 EPR signal of NO-bound cis-thiolate-ligated [Fe(S(Me(2))N(4)(tren)(NO)](+) (2; g = 4.44, 3.54, 1.97), the isotopically sensitive ν(NO)(ν((15)NO)) stretching frequency (1685(1640) cm(-1)), and the 0.05 Å decrease in Fe-S bond length are shown to be consistent with the oxidative addition of NO to Fe(II) to afford an Fe(III)-NO(-) {FeNO}(7) species containing high-spin (S = 5/2) Fe(III) antiferromagnetically coupled to NO(-) (S = 1). The cis versus trans positioning of the thiolate does not appear to influence these properties. Although it has yet to be crystallographically characterized, SOR-NO is presumed to possess a bent Fe-NO similar to that of 2 (Fe-N-O = 151.7(4)°). The N-O bond is shown to be more activated in 2 relative to N- and O-ligated {FeNO}(7) complexes, and this is attributed to the electron-donating properties of the thiolate ligand. Hydrogen-bonding to the cysteinate sulfur attenuates N-O bond activation in SOR, as shown by its higher ν(NO) frequency (1721 cm(-1)). In contrast, the ν(O-O) frequency of the SOR peroxo intermediate and its analogues is not affected by H-bonds to the cysteinate sulfur or other factors influencing the Fe-SR bond strength; these only influence the ν(Fe-O) frequency. Reactions between 1 and NO(2)(-) are shown to result in the proton-dependent heterolytic cleavage of an N-O bond. The mechanism of this reaction is proposed to involve both Fe(II)-NO(2)(-) and {FeNO}(6) intermediates similar to those implicated in the mechanism of NiR-promoted NO(2)(-) reduction.

Indexed as

ProtonsBinding SitesBiomimetic MaterialsElectronsLigandsMagneticsModels, MolecularMolecular ConformationNitric OxideNitritesNitrogenOxidation-ReductionOxidoreductasesOxygenSuperoxidesVibrationLigandsNitric OxideNitritesNitrogenOxidoreductasesOxygenProtonssuperoxide reductaseSuperoxides

Identifiers

PMID21207999
PMCPMC3178331
OpenAlexW2016061901

What OpenQuestion holds

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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.