Evidence map›Paper›PMID 19816718›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2010

Multicopper oxidases: a workshop on copper coordination chemistry, electron transfer, and metallophysiology.

Daniel J Kosman

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
19.4field-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

64 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
  2. Genome-Wide Identification and Salt Tolerance Analysis of theInternational journal of molecular sciences · 2026
    Article
  3. Review
  4. Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Review
  5. Article
  6. Flexible active-site loops fine-tune substrate specificity of hyperthermophilic metallo-oxidases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. A Fluoran-Based CuJournal of fluorescence · 2020
    Article
  13. Article
  14. Multicopper Oxidases inJournal of fungi (Basel, Switzerland) · 2020
    Review
  15. Article
  16. Article
  17. The Altered Expression ofFrontiers in plant science · 2019
    Article
  18. Review
  19. Article
  20. Article

4 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

1 author at 1 institution in 1 country.

Daniel J KosmanDepartment of Biochemistry, The University at Buffalo, NY 14214, USA. camkos@buffalo.edu
University at Buffalo, State University of New York · US

Funding

Managing ionic iron: ferri-reduction, ferro-oxidation and iron permeationR01DK053820 · NIDDK · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KOSMAN, DANIEL J. · 1999 to 2016
$4.0M
NIDDK NIH HHS R01 DK053820
6 · The paper itself

Abstract

Multicopper oxidases (MCOs) are unique among copper proteins in that they contain at least one each of the three types of biologic copper sites, type 1, type 2, and the binuclear type 3. MCOs are descended from the family of small blue copper proteins (cupredoxins) that likely arose as a complement to the heme-iron-based cytochromes involved in electron transport; this event corresponded to the aerobiosis of the biosphere that resulted in the conversion of Fe(II) to Fe(III) as the predominant redox state of this essential metal and the solubilization of copper from Cu(2)S to Cu(H(2)O)( n ) (2+). MCOs are encoded in genomes in all three kingdoms and play essential roles in the physiology of essentially all aerobes. With four redox-active copper centers, MCOs share with terminal copper-heme oxidases the ability to catalyze the four-electron reduction of O(2) to two molecules of water. The electron transfers associated with this reaction are both outer and inner sphere in nature and their mechanisms have been fairly well established. A subset of MCO proteins exhibit specificity for Fe(2+), Cu(+), and/or Mn(2+) as reducing substrates and have been designated as metallooxidases. These enzymes, in particular the ferroxidases found in all fungi and metazoans, play critical roles in the metal metabolism of the expressing organism.

Indexed as

Amino Acid SequenceAnimalsCopperElectron TransportEvolution, MolecularHumansOxidoreductasesProtein Structure, TertiaryWaterCoppercopper oxidaseOxidoreductasesWater

Identifiers

PMID19816718
OpenAlexW2007682090

What OpenQuestion holds

Textmetadata
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.