Evidence map›Paper›PMID 25314114›Full record

ArticleAngewandte Chemie (International ed. in English)2014

Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase.

Soi Bui, David von Stetten, Pablo G Jambrina, Thierry Prangé, Nathalie Colloc'h, Daniele de Sanctis, Antoine Royant, Edina Rosta, Roberto A Steiner

Open access · bronzeAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  5. Neutron crystallographic refinement with REFMAC5 from the CCP4 suite.Acta crystallographica. Section D, Structural biology · 2023
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  10. Introduction to the virtual thematic issue on room-temperature biological crystallography.Acta crystallographica. Section F, Structural biology communications · 2023
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  11. Article
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  14. Computational Approach for Rational Design of Fusion Uricase with PAS Sequences.International journal of molecular and cellular medicine · 2020
    Article
  15. Article
  16. Article
  17. Estimate your dose: RADDOSE-3D.Protein science : a publication of the Protein Society · 2018
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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

9 authors at 4 institutions in 2 countries.

Soi BuiRandall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL (UK).
David von Stetten
Pablo G Jambrina
Thierry Prangé
Nathalie Colloc'h
Daniele de Sanctis
Antoine Royant
Edina Rosta
Roberto A Steiner
King's College London · GBCentre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · FRDélégation Paris 5 · FR

Funding

Biotechnology and Biological Sciences Research Council BB/I020411/1
6 · The paper itself

Abstract

Cofactor-free oxidases and oxygenases promote and control the reactivity of O2 with limited chemical tools at their disposal. Their mechanism of action is not completely understood and structural information is not available for any of the reaction intermediates. Near-atomic resolution crystallography supported by in crystallo Raman spectroscopy and QM/MM calculations showed unambiguously that the archetypical cofactor-free uricase catalyzes uric acid degradation via a C5(S)-(hydro)peroxide intermediate. Low X-ray doses break specifically the intermediate C5-OO(H) bond at 100 K, thus releasing O2 in situ, which is trapped above the substrate radical. The dose-dependent rate of bond rupture followed by combined crystallographic and Raman analysis indicates that ionizing radiation kick-starts both peroxide decomposition and its regeneration. Peroxidation can be explained by a mechanism in which the substrate radical recombines with superoxide transiently produced in the active site.

Indexed as

CatalysisOxidoreductasesOxygenPeroxidesSubstrate SpecificityOxidoreductasesOxygenPeroxidesdioxygenenzymatic mechanismsoxidasesreaction intermediatesstructural enzymology

Identifiers

PMID25314114
PMCPMC4502973
OpenAlexW2109273153

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.