Evidence map›Paper›PMID 24615282›Full record

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

A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases.

Andrew J Fielding, John D Lipscomb, Lawrence Que

Abstract readReview
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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Mimicking Extradiol Dioxygenase Reactivity on Iridium.Journal of the American Chemical Society · 2026
    Article
  2. Vitamin BACS central science · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. The role of halogen substituents and substrate pKJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  10. Nuclear Resonance Vibrational Spectroscopy Definition of OJournal of the American Chemical Society · 2018
    Article
  11. Probing Hydrogen Bonding Interactions to Iron-Oxido/Hydroxido Units byAngewandte Chemie (International ed. in English) · 2018
    Article
  12. Review
  13. On the Structure and Reaction Mechanism of Human Acireductone Dioxygenase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018
    Article
  14. Article
  15. 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
  16. Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors.

Andrew J FieldingDepartment of Chemistry, University of Minnesota, Minneapolis, MN, 55455, USA.
John D Lipscomb
Lawrence Que

Funding

OXYGENASE ENZYME MECHANISMR01GM024689 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI LIPSCOMB, JOHN D · 1985 to 2016
$3.8M
OXYGENASE ENZYME MECHANISMR37GM024689 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI LIPSCOMB, JOHN D · 1994 to 2003
$1.1M
NON-HEME IRON OXYGEN ACTIVATION IN ENZYMES AND MODELSR01GM033162 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI QUE, LAWRENCE · 1985 to 1999
–
NIGMS NIH HHS R01 GM024689NIGMS NIH HHS R01 GM033162NIGMS NIH HHS R37 GM024689
6 · The paper itself

Abstract

Extradiol-cleaving catechol dioxygenases function by binding both the organic substrate and O2 at a divalent metal center in the active site. They have proven to be a particularly versatile group of enzymes with which to study the O2 activation process. Here, recent studies of homoprotocatechuate 2,3-dioxygenase are summarized, showing how nature can utilize the enzyme structure and the properties of the metal and the substrate to select among many possible chemical paths to achieve both specificity and efficiency. Possible intermediates in the mechanism have been trapped by swapping active-site metals, introducing active-site amino acid substituted variants, and using substrates with different electron-donating capacities. Although each of these intermediates could form part of a viable reaction pathway, kinetic measurements significantly limit the likely candidates. Structural, kinetic, spectroscopic, and computational analyses of the various intermediates shed light on how catalytic efficiency can be achieved.

Indexed as

Binding SitesCatalysisCrystallography, X-RayDioxygenasesKineticsModels, MolecularOxygenases3,4-dihydroxyphenylacetate 2,3-dioxygenaseDioxygenasesextradiol dioxygenaseOxygenases

Identifiers

PMID24615282
PMCPMC4039383

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.