Evidence map›Paper›PMID 25437493›Full record

ArticleBiochemistry2015

A dimeric chlorite dismutase exhibits O2-generating activity and acts as a chlorite antioxidant in Klebsiella pneumoniae MGH 78578.

Arianna I Celis, Zachary Geeraerts, David Ngmenterebo, Melodie M Machovina, Richard C Kurker, Kumar Rajakumar, Anabella Ivancich, Kenton R Rodgers, Gudrun S Lukat-Rodgers, Jennifer L DuBois

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Parapatric speciation ofFrontiers in microbiology · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Active Sites of OBiochemistry · 2017
    Article
  18. 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

10 authors at 4 institutions in 2 countries.

Arianna I CelisDepartment of Chemistry and Biochemistry, Montana State University , Bozeman, Montana 59715, United States.
Zachary Geeraerts
David Ngmenterebo
Melodie M Machovina
Richard C Kurker
Kumar Rajakumar
Anabella Ivancich
Kenton R Rodgers
Gudrun S Lukat-Rodgers
Jennifer L DuBois
Montana State University · USNorth Dakota State University · USUniversity of Notre Dame · USCEA Paris-Saclay · FR

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
Understanding the diverse biochemistry of the chlorite dismutase family: from O2 to hemeR01GM090260 · NIGMS · UNIVERSITY OF NOTRE DAME · PI DUBOIS, JENNIFER L · 2009 to 2018
$2.7M
Study of heme uptake and transport proteins from P. aerugenosa and S. dysenteriaeR15AI072719 · NIAID · NORTH DAKOTA STATE UNIVERSITY · PI RODGERS, KENTON · 2007 to 2011
$707k
Determining the structural basis for the mechanism of catalytic O2 evolution by tR15GM094039 · NIGMS · NORTH DAKOTA STATE UNIVERSITY · PI LUKAT-RODGERS, GUDRUN SUSANNE · 2010 to 2010
$431k
NIAID NIH HHS AI072719NIAID NIH HHS R15 AI072719NIGMS NIH HHS GM094039NIGMS NIH HHS R01 GM090260NIGMS NIH HHS R01GM090260NIGMS NIH HHS R15 GM094039NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

Chlorite dismutases (Clds) convert chlorite to O2 and Cl(-), stabilizing heme in the presence of strong oxidants and forming the O═O bond with high efficiency. The enzyme from the pathogen Klebsiella pneumoniae (KpCld) represents a subfamily of Clds that share most of their active site structure with efficient O2-producing Clds, even though they have a truncated monomeric structure, exist as a dimer rather than a pentamer, and come from Gram-negative bacteria without a known need to degrade chlorite. We hypothesized that KpCld, like others in its subfamily, should be able to make O2 and may serve an in vivo antioxidant function. Here, it is demonstrated that it degrades chlorite with limited turnovers relative to the respiratory Clds, in part because of the loss of hypochlorous acid from the active site and destruction of the heme. The observation of hypochlorous acid, the expected leaving group accompanying transfer of an oxygen atom to the ferric heme, is consistent with the more open, solvent-exposed heme environment predicted by spectroscopic measurements and inferred from the crystal structures of related proteins. KpCld is more susceptible to oxidative degradation under turnover conditions than the well-characterized Clds associated with perchlorate respiration. However, wild-type K. pneumoniae has a significant growth advantage in the presence of chlorate relative to a Δcld knockout strain, specifically under nitrate-respiring conditions. This suggests that a physiological function of KpCld may be detoxification of endogenously produced chlorite.

Indexed as

AntioxidantsChloridesHumansKlebsiella InfectionsKlebsiella pneumoniaeModels, MolecularOxidoreductasesOxygenProtein MultimerizationAntioxidantsChlorideschloritechlorite dismutaseOxidoreductasesOxygen

Identifiers

PMID25437493
PMCPMC4303309
OpenAlexW2031202745

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.