Evidence map›Paper›PMID 27921179›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017

Activation of dioxygen by copper metalloproteins and insights from model complexes.

David A Quist, Daniel E Diaz, Jeffrey J Liu, Kenneth D Karlin

Open access · greenAbstract readReview
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
14.6field-weighted citation impact, top 1% 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

89 citing papers in PubMed, 228 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanism of OACS central science · 2025
    Article
  8. Article
  9. Copper-chelating natural products.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Cu-PromotedInorganic chemistry · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Intramolecular Phenolic H-Atom Abstraction by a NJournal of the American Chemical Society · 2024
    Article
  20. Article

29 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

David A QuistDepartment of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA.
Daniel E DiazDepartment of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA.
Jeffrey J LiuDepartment of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA.
Kenneth D KarlinDepartment of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA. karlin@jhu.edu.
Johns Hopkins University · US

Funding

NEW COPPER(I) CHEMISTRY-MODELS FOR METALLOPROTEINSR01GM028962 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI KARLIN, KENNETH D. · 1985 to 2020
$6.7M
Heme/Copper and Heme/Nonheme Iron O(2) and NO ReactivityR01GM060353 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KARLIN, KENNETH D. · 2000 to 2020
$5.9M
NIGMS NIH HHS R01 GM028962NIGMS NIH HHS R01 GM060353
6 · The paper itself

Abstract

Nature uses dioxygen as a key oxidant in the transformation of biomolecules. Among the enzymes that are utilized for these reactions are copper-containing metalloenzymes, which are responsible for important biological functions such as the regulation of neurotransmitters, dioxygen transport, and cellular respiration. Enzymatic and model system studies work in tandem in order to gain an understanding of the fundamental reductive activation of dioxygen by copper complexes. This review covers the most recent advancements in the structures, spectroscopy, and reaction mechanisms for dioxygen-activating copper proteins and relevant synthetic models thereof. An emphasis has also been placed on cofactor biogenesis, a fundamentally important process whereby biomolecules are post-translationally modified by the pro-enzyme active site to generate cofactors which are essential for the catalytic enzymatic reaction. Significant questions remaining in copper-ion-mediated O

Indexed as

AnimalsCatalytic DomainCopperHumansMetalloproteinsOxygenCopperMetalloproteinsOxygenCofactor biogenesisCopperCopper enzymesDioxygen activationEnzymatic mechanisms

Identifiers

PMID27921179
PMCPMC5600896
OpenAlexW2560172664

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.