Evidence map›Paper›PMID 40458033›Full record

ArticleThe FEBS journal2025

Biochemical and structural characterization of chlorite dismutase enzyme from Pseudomonas aeruginosa.

Dimitrios V Nokas, Eleni K Panagiotopoulou, Antonios I Kapogiannatos, Georgios E Premetis, Nikolaos E Labrou, Eleni K Efthimiadou, Anastassios C Papageorgiou, Evangelia G Chronopoulou

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Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Dimitrios V NokasLaboratory of Enzyme Technology, Department of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Greece.
Eleni K PanagiotopoulouLaboratory of Enzyme Technology, Department of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Greece.ORCID https://orcid.org/0009-0006-8737-1489
Antonios I KapogiannatosLaboratory of Enzyme Technology, Department of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Greece.
Georgios E PremetisLaboratory of Enzyme Technology, Department of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Greece.
Nikolaos E LabrouLaboratory of Enzyme Technology, Department of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Greece.ORCID https://orcid.org/0000-0003-1925-9867
Eleni K EfthimiadouInorganic Chemistry Laboratory, Department of Chemistry, National and Kapodistrian University of Athens, Zografou, Greece.
Anastassios C PapageorgiouTurku Bioscience Centre, University of Turku and Åbo Akademi University, Finland.
Evangelia G ChronopoulouLaboratory of Enzyme Technology, Department of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Greece.ORCID https://orcid.org/0000-0001-7269-2817

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Industrialization and urbanization have caused serious contamination of water bodies, and the removal of chemical contaminants has become a major challenge. Chlorite is a harmful anthropogenic compound with a serious environmental impact and has been detected in groundwater, drinking water, and soil. Enzymes are considered sustainable tools for bioremediation, with chlorite dismutase (Cld) being a notable example. This enzyme has unique properties owing to the rare dioxygen bond formation that it catalyzes. In the present study, we report the cloning, biochemical, and structural characterization of the dimeric Cld from Pseudomonas aeruginosa (PaCld). PaCld is a heme b oxidoreductase that can decompose chlorite (

Indexed as

Bacterial ProteinsOxidoreductasesPseudomonas aeruginosaAmino Acid SequenceCatalytic DomainChloridesCloning, MolecularCrystallography, X-RayKineticsModels, MolecularOxygenBacterial ProteinsChlorideschloritechlorite dismutaseOxidoreductasesOxygenchlorite degradationchlorite dismutaseCld structureCld thermostabilityheme b‐containing oxidoreductases

Identifiers

PMID40458033
PMCPMC12525007

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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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.