Evidence map›Paper›PMID 24632343›Full record

ArticleJournal of inorganic biochemistry2014

Mechanism of reaction of chlorite with mammalian heme peroxidases.

Christa Jakopitsch, Katharina F Pirker, Jörg Flemmig, Stefan Hofbauer, Denise Schlorke, Paul G Furtmüller, Jürgen Arnhold, Christian Obinger

Open access · hybridAbstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

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  4. 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
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  13. Reactions of aquacobalamin and cob(II)alamin with chlorite and chlorine dioxide.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
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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

8 authors at 2 institutions in 2 countries.

Christa JakopitschDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Katharina F PirkerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Jörg FlemmigInstitute for Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Härtelstr 16-18, D-04107 Leipzig, Germany; Translational Centre for Regenerative Medicine, University of Leipzig, Philipp-Rosenthal-Strasse 55, D-04103 Leipzig, Germany.
Stefan HofbauerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Denise SchlorkeInstitute for Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Härtelstr 16-18, D-04107 Leipzig, Germany.
Paul G FurtmüllerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Jürgen ArnholdInstitute for Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Härtelstr 16-18, D-04107 Leipzig, Germany; Translational Centre for Regenerative Medicine, University of Leipzig, Philipp-Rosenthal-Strasse 55, D-04103 Leipzig, Germany.
Christian ObingerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria. Electronic address: christian.obinger@boku.ac.at.
BOKU University · ATLeipzig University · DE

Funding

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

Abstract

This study demonstrates that heme peroxidases from different superfamilies react differently with chlorite. In contrast to plant peroxidases, like horseradish peroxidase (HRP), the mammalian counterparts myeloperoxidase (MPO) and lactoperoxidase (LPO) are rapidly and irreversibly inactivated by chlorite in the micromolar concentration range. Chlorite acts as efficient one-electron donor for Compound I and Compound II of MPO and LPO and reacts with the corresponding ferric resting states in a biphasic manner. The first (rapid) phase is shown to correspond to the formation of a MPO-chlorite high-spin complex, whereas during the second (slower) phase degradation of the prosthetic group was observed. Cyanide, chloride and hydrogen peroxide can block or delay heme bleaching. In contrast to HRP, the MPO/chlorite system does not mediate chlorination of target molecules. Irreversible inactivation is shown to include heme degradation, iron release and decrease in thermal stability. Differences between mammalian peroxidases and HRP are discussed with respect to differences in active site architecture and heme modification.

Indexed as

AnimalsCalorimetry, Differential ScanningCatalytic DomainCattleChloridesElectron Spin Resonance SpectroscopyHemeHorseradish PeroxidaseHumansKineticsLactoperoxidaseOxidation-ReductionPeroxidaseProtein Structure, SecondaryReducing AgentsChlorideschloriteHemeHorseradish PeroxidaseLactoperoxidasePeroxidaseReducing AgentsChlorine dioxideChloriteHypochlorous acidLactoperoxidaseMyeloperoxidaseOxoferin

Identifiers

PMID24632343
PMCPMC4003552
OpenAlexW2018809837

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.