Evidence map›Paper›PMID 24519858›Full record

ReviewBiotechnology journal2014

Chlorite dismutases - a heme enzyme family for use in bioremediation and generation of molecular oxygen.

Stefan Hofbauer, Irene Schaffner, Paul G Furtmüller, Christian Obinger

Open access · bronzeAbstract readReview
In one paragraph

Review in Biotechnology journal, 2014. 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
4.8field-weighted citation impact, top 5% 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, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. The chlorite adduct of aquacobalamin: contrast with chlorite dismutase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  4. Review
  5. Article
  6. Parapatric speciation ofFrontiers in microbiology · 2023
    Article
  7. A genetically encoded system for oxygen generation in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020
    Article
  15. Article
  16. A traffic light enzyme: acetate binding reversibly switches chlorite dismutase from a red- to a green-colored heme protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  17. 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

4 authors at 1 institution in 1 country.

Stefan HofbauerDepartment of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU, University of Natural Resources and Life Sciences, Vienna, Austria.
Irene Schaffner
Paul G Furtmüller
Christian Obinger
BOKU University · AT

Funding

Austrian Science Fund FWF P 25270Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Chlorite is a serious environmental concern, as rising concentrations of this harmful anthropogenic compound have been detected in groundwater, drinking water, and soil. Chlorite dismutases (Clds) are therefore important molecules in bioremediation as Clds catalyze the degradation of chlorite to chloride and molecular oxygen. Clds are heme b-containing oxidoreductases present in numerous bacterial and archaeal phyla. This review presents the phylogeny of functional Clds and Cld-like proteins, and demonstrates the close relationship of this novel enzyme family to the recently discovered dye-decolorizing peroxidases. The available X-ray structures, biophysical and enzymatic properties, as well as a proposed reaction mechanism, are presented and critically discussed. Open questions about structure-function relationships are addressed, including the nature of the catalytically relevant redox and reaction intermediates and the mechanism of inactivation of Clds during turnover. Based on analysis of currently available data, chlorite dismutase from "Candidatus Nitrospira defluvii" is suggested as a model Cld for future application in biotechnology and bioremediation. Additionally, Clds can be used in various applications as local generators of molecular oxygen, a reactivity already exploited by microbes that must perform aerobic metabolic pathways in the absence of molecular oxygen. For biotechnologists in the field of chemical engineering and bioremediation, this review provides the biochemical and biophysical background of the Cld enzyme family as well as critically assesses Cld's technological potential.

Indexed as

Biodegradation, EnvironmentalOxidoreductasesOxygenArchaeal ProteinsBacterial ProteinsChloridesHemeWater Pollutants, ChemicalArchaeal ProteinsBacterial ProteinsChlorideschloritechlorite dismutaseHemeOxidoreductasesOxygenWater Pollutants, ChemicalBioremediationChlorite degradationChlorite dismutaseEnzymologyMetalloprotein

Identifiers

PMID24519858
PMCPMC4162996
OpenAlexW2124173751

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.