Evidence map›Paper›PMID 24281855›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2014

Peroxomanganese complexes as an aid to understanding redox-active manganese enzymes.

Domenick F Leto, Timothy A Jackson

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Investigating Ligand Sphere Perturbations on MnMolecules (Basel, Switzerland) · 2024
    Article
  2. Article
  3. Article
  4. Steric control of dioxygen activation pathways for MnDalton transactions (Cambridge, England : 2003) · 2019
    Article
  5. A MnAngewandte Chemie (International ed. in English) · 2019
    Article
  6. MnDalton transactions (Cambridge, England : 2003) · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Oxygen activation by mononuclear Mn, Co, and Ni centers in biology and synthetic complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Review
  11. Article
  12. Article
  13. 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.

Domenick F LetoDepartment of Chemistry and Center for Environmentally Beneficial Catalysis, University of Kansas, Lawrence, KS, 66045, USA.
Timothy A Jackson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the past 7 years, there have been a significant number of studies describing the structural and electronic properties, as well as the chemical reactivity, of synthetic peroxomanganese adducts. Many redox-active manganese enzymes, including manganese-containing superoxide dismutases, extradiol catechol dioxygenases, and ribonucleotide reductases, are proposed to feature peroxomanganese intermediates in their catalytic cycles. The recent efforts to model these intermediates using synthetic complexes have thus provided a strong complement to mechanistic studies of the enzymes. This review provides both a summary and a perspective of work in this area, with an emphasis on the relationship between geometric and electronic structure and chemical reactivity for η(2)-peroxomanganese(III) and η(1)-alkylperoxomanganese(III) adducts.

Indexed as

AnimalsCarboxy-LyasesCatalaseDioxygenasesHumansManganeseModels, MolecularOxidation-ReductionOxidoreductasesRibonucleotide ReductasesSpectrum AnalysisSuperoxide DismutaseCarboxy-LyasesCatalaseDioxygenasesManganeseoxalate decarboxylaseoxalate oxidaseOxidoreductasesRibonucleotide ReductasesSuperoxide Dismutase

Identifiers

What OpenQuestion holds

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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.