Phenol-driven cometabolic degradation of cis-1,2-dichloroethene (cDCE): insights from Acinetobacter pittii and Ectopseudomonas alcaliphila

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F25%3A00641711" target="_blank" >RIV/68378050:_____/25:00641711 - isvavai.cz</a>

Alternative codes found

RIV/46747885:24620/25:00014429 RIV/60461373:22320/25:43932497 RIV/60461373:22330/25:43932497

Result on the web

<a href="https://doi.org/10.1186/s12302-025-01237-z" target="_blank" >https://doi.org/10.1186/s12302-025-01237-z</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1186/s12302-025-01237-z" target="_blank" >10.1186/s12302-025-01237-z</a>

Result language

angličtina

Original language name

Phenol-driven cometabolic degradation of cis-1,2-dichloroethene (cDCE): insights from Acinetobacter pittii and Ectopseudomonas alcaliphila

Original language description

Accumulation of xenobiotic chlorinated ethenes (CEs) at legacy industrial soil and groundwater sites around the world is a pressing environmental and public health issue. Understanding the biochemical pathways through which microorganisms degrade cDCE is key to developing cost-effective, sustainable bioremediation strategies for CE contamination. Two strains, Acinetobacter pittii CEP14 and Ectopseudomonas alcaliphila JAB1, isolated from contaminated industrial sites, have demonstrated the ability to cometabolically degrade cDCE in the presence of phenol. In this study, we integrate transcriptomics, using differential gene expression analysis to pinpoint genes induced during cDCE co-metabolism, with proteomics to confirm protein-level expression. We use heterologous expression experiments to demonstrate that phenol monooxygenase is responsible for oxidising cDCE in both strains. Furthermore, we show that CEP14 and JAB1 alpha-subunits share 71.4% identity with each other but only 14.6-26.5% identity with established monooxygenases with known cDCE-oxidising activity, highlighting the diversity of enzymes that may be capable of cometabolic cDCE degradation. Finally, we hypothesise on a two-branch phenol monooxygenase-mediated cDCE degradation pathway in which the chemical degradative intermediates 2,2-dichloroacetaldehyde and cDCE epoxides are formed. This study sheds light on the biochemical mechanisms by which monoaromatic compounds can enhance the biodegradation of cDCE and demonstrates the potential utilisation of strains CEP14 and JAB1 for the biodegradation of cDCE.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Environmental Sciences Europe

ISSN

2190-4707

e-ISSN

2190-4715

Volume of the periodical

37

Issue of the periodical within the volume

1

Country of publishing house

CH - SWITZERLAND

Number of pages

15

Pages from-to

196

UT code for WoS article

001609529600004

EID of the result in the Scopus database

2-s2.0-105021089092