Evidence map›Paper›PMID 22814765›Full record

ArticleDalton transactions (Cambridge, England : 2003)2012

Sulfur oxygenation in biomimetic non-heme iron-thiolate complexes.

Alison C McQuilken, David P Goldberg

Abstract read
In one paragraph

Article in Dalton transactions (Cambridge, England : 2003), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Spectroscopic, electrochemical, and kinetic trends in Fe(III)-thiolate disproportionation near physiologic pH.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  3. Article
  4. Article
  5. The roles of chalcogenides in OChemical science · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Metal-Assisted Oxo Atom Addition to an Fe(III) Thiolate.Journal of the American Chemical Society · 2017
    Article
  11. Article
  12. Review
  13. Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs.Protein science : a publication of the Protein Society · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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.

Alison C McQuilkenDepartment of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
David P Goldberg

Funding

Synthetic Models of N/S-Ligated Metal Centers in BiologyR01GM062309 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GOLDBERG, DAVID P · 2001 to 2010
$2.2M
NIGMS NIH HHS GM62309NIGMS NIH HHS R01 GM062309
6 · The paper itself

Abstract

The S-oxygenation of cysteine with dioxygen to give cysteine sulfinic acid occurs at the non-heme iron active site of cysteine dioxygenase. Similar S-oxygenation events occur in other non-heme iron enzymes, including nitrile hydratase and isopenicillin N synthase, and these enzymes have inspired the development of a class of [N(x)S(y)]-Fe model complexes. Certain members of this class have provided some intriguing examples of S-oxygenation, and this article summarizes these results, focusing on the non-heme iron(II/III)-thiolate model complexes that are known to react with O(2) or other O-atom transfer oxidants to yield sulfur oxygenates. Key aspects of the synthesis, structure, and reactivity of these systems are presented, along with any mechanistic information available on the oxygenation reactions. A number of iron(III)-thiolate complexes react with O(2) to give S-oxygenates, and the degree to which the thiolate sulfur donors are oxidized varies among the different complexes, depending upon the nature of the ligand, metal geometry, and spin state. The first examples of iron(II)-thiolate complexes that react with O(2) to give selective S-oxygenation are just emerging. Mechanistic information on these transformations is limited, with isotope labeling studies providing much of the current mechanistic data. The many questions that remain unanswered for both models and enzymes provide strong motivation for future work in this area.

Indexed as

Biomimetic MaterialsCatalytic DomainCoordination ComplexesCrystallography, X-RayFerric CompoundsFerrous CompoundsHemeHydro-LyasesMolecular ConformationOxidoreductasesOxygenSulfhydryl CompoundsSulfurCoordination ComplexesFerric CompoundsFerrous CompoundsHemeHydro-Lyasesisopenicillin N synthetasenitrile hydrataseOxidoreductasesOxygenSulfhydryl CompoundsSulfur

Identifiers

PMID22814765
PMCPMC3454461

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.