Evidence map›Paper›PMID 20463026›Full record

ArticleThe Journal of biological chemistry2010

Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase.

José R R Cussiol, Thiago G P Alegria, Luke I Szweda, Luis E S Netto

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification of the organic peroxide scavenging system ofApplied and environmental microbiology · 2024
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  4. Review
  5. Review
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  7. RpoS and the bacterial general stress response.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  8. Genetic Basis ofLife (Basel, Switzerland) · 2023
    Article
  9. Article
  10. Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022
    Review
  11. Disruption of theJournal of bacteriology · 2022
    Article
  12. Article
  13. Regulation ofMicroorganisms · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Identification of Plasmid-Encoded sRNAs in aFrontiers in microbiology · 2018
    Article
  19. Article
  20. 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

4 authors at 3 institutions in 3 countries.

José R R CussiolDepartamento de Genética e Biologia Evolutiva, Instituto de Biociencias, Universidade de Sao Paulo, Rua do Matão 277, São Paulo 05508-900, Brazil.
Thiago G P Alegria
Luke I Szweda
Luis E S Netto
Universidade de São Paulo · BRInstituto de Geociencias · ESOklahoma Medical Research Foundation · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Ohr (organic hydroperoxide resistance) family of 15-kDa Cys-based, thiol-dependent peroxidases is central to the bacterial response to stress induced by organic hydroperoxides but not by hydrogen peroxide. Ohr has a unique three-dimensional structure and requires dithiols, but not monothiols, to support its activity. However, the physiological reducing system of Ohr has not yet been identified. Here we show that lipoylated enzymes present in the bacterial extracts of Xylella fastidiosa interacted physically and functionally with this Cys-based peroxidase, whereas thioredoxin and glutathione systems failed to support Ohr peroxidase activity. Furthermore, we could reconstitute in vitro three lipoyl-dependent systems as the Ohr physiological reducing systems. We also showed that OsmC from Escherichia coli, an orthologue of Ohr from Xylella fastidiosa, is specifically reduced by lipoyl-dependent systems. These results represent the first description of a Cys-based peroxidase that is directly reduced by lipoylated enzymes.

Indexed as

Bacterial ProteinsEscherichia coliEscherichia coli ProteinsKineticsLipoylationModels, BiologicalOxidation-ReductionPeroxidasesProtein BindingRepressor ProteinsSubstrate SpecificityXylellaBacterial ProteinsEscherichia coli ProteinsosmC protein, E coliPeroxidasesperoxide repressor proteinsRepressor Proteins

Identifiers

PMID20463026
PMCPMC2903379
OpenAlexW2046711233

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.