Evidence map›Paper›PMID 21808032›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Homogeneous catalytic O2 reduction to water by a cytochrome c oxidase model with trapping of intermediates and mechanistic insights.

Zakaria Halime, Hiroaki Kotani, Yuqi Li, Shunichi Fukuzumi, Kenneth D Karlin

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
10.0field-weighted citation impact, top 2% 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

31 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Structural Determination of an Unusual CuChemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  7. Selectivity-Determining Steps in OJournal of the American Chemical Society · 2020
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Isocyanide or nitrosyl complexation to hemes with varying tethered axial base ligand donors: synthesis and characterization.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  17. Article
  18. Article
  19. Article
  20. Nitric oxide generation from heme/copper assembly mediated nitrite reductase activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    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

5 authors at 4 institutions in 3 countries.

Zakaria HalimeDepartment of Material and Life Science, Division of Advanced Science and Biotechnology, Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan.
Hiroaki Kotani
Yuqi Li
Shunichi Fukuzumi
Kenneth D Karlin
Japan Science and Technology Agency · JPEwha Womans University · KRJohns Hopkins University · USOsaka University · JP

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
BIOINORGANIC COPPER COORDINATION CHEMISTRYR37GM028962 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KARLIN, KENNETH D. · 1993 to 2002
$882k
NIGMS NIH HHS GM28962NIGMS NIH HHS R01 GM028962NIGMS NIH HHS R01 GM060353NIGMS NIH HHS R37 GM028962
6 · The paper itself

Abstract

An efficient and selective four-electron plus four-proton (4e(-)/4H(+)) reduction of O(2) to water by decamethylferrocene and trifluoroacetic acid can be catalyzed by a synthetic analog of the heme a(3)/Cu(B) site in cytochrome c oxidase ((6)LFeCu) or its Cu-free version ((6)LFe) in acetone. A detailed mechanistic-kinetic study on the homogeneous catalytic system reveals spectroscopically detectable intermediates and that the rate-determining step changes from the O(2)-binding process at 25 °C room temperature (RT) to the O-O bond cleavage of a newly observed Fe(III)-OOH species at lower temperature (-60 °C). At RT, the rate of O(2)-binding to (6)LFeCu is significantly faster than that for (6)LFe, whereas the rates of the O-O bond cleavage of the Fe(III)-OOH species observed (-60 °C) with either the (6)LFeCu or (6)LFe catalyst are nearly the same. Thus, the role of the Cu ion is to assist the heme and lead to faster O(2)-binding at RT. However, the proximate Cu ion has no effect on the O-O bond cleavage of the Fe(III)-OOH species at low temperature.

Indexed as

BiocatalysisModels, MolecularBiomechanical PhenomenaElectronsElectron Transport Complex IVOxidation-ReductionOxygenSpectrophotometry, UltravioletTemperatureWaterElectron Transport Complex IVOxygenWater

Identifiers

PMID21808032
PMCPMC3161539
OpenAlexW2053757872

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.