• Medientyp: E-Artikel
  • Titel: Anaerobic Activation of p -Cymene in Denitrifying Betaproteobacteria: Methyl Group Hydroxylation versus Addition to Fumarate
  • Beteiligte: Strijkstra, Annemieke; Trautwein, Kathleen; Jarling, René; Wöhlbrand, Lars; Dörries, Marvin; Reinhardt, Richard; Drozdowska, Marta; Golding, Bernard T.; Wilkes, Heinz; Rabus, Ralf
  • Erschienen: American Society for Microbiology, 2014
  • Erschienen in: Applied and Environmental Microbiology
  • Sprache: Englisch
  • DOI: 10.1128/aem.02385-14
  • ISSN: 0099-2240; 1098-5336
  • Schlagwörter: Ecology ; Applied Microbiology and Biotechnology ; Food Science ; Biotechnology
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  • Beschreibung: <jats:title>ABSTRACT</jats:title> <jats:p> The betaproteobacteria “ <jats:named-content content-type="genus-species">Aromatoleum aromaticum</jats:named-content> ” pCyN1 and “ <jats:named-content content-type="genus-species">Thauera</jats:named-content> ” sp. strain pCyN2 anaerobically degrade the plant-derived aromatic hydrocarbon <jats:italic>p</jats:italic> -cymene (4-isopropyltoluene) under nitrate-reducing conditions. Metabolite analysis of <jats:italic>p</jats:italic> -cymene-adapted “ <jats:named-content content-type="genus-species">A. aromaticum</jats:named-content> ” pCyN1 cells demonstrated the specific formation of 4-isopropylbenzyl alcohol and 4-isopropylbenzaldehyde, whereas with “ <jats:named-content content-type="genus-species">Thauera</jats:named-content> ” sp. pCyN2, exclusively 4-isopropylbenzylsuccinate and tentatively identified (4-isopropylphenyl)itaconate were observed. 4-Isopropylbenzoate in contrast was detected with both strains. Proteogenomic investigation of <jats:italic>p</jats:italic> -cymene- versus succinate-adapted cells of the two strains revealed distinct protein profiles agreeing with the different metabolites formed from <jats:italic>p</jats:italic> -cymene. “ <jats:named-content content-type="genus-species">A. aromaticum</jats:named-content> ” pCyN1 specifically produced (i) a putative <jats:italic>p</jats:italic> -cymene dehydrogenase (CmdABC) expected to hydroxylate the benzylic methyl group of <jats:italic>p</jats:italic> -cymene, (ii) two dehydrogenases putatively oxidizing 4-isopropylbenzyl alcohol (Iod) and 4-isopropylbenzaldehyde (Iad), and (iii) the putative 4-isopropylbenzoate-coenzyme A (CoA) ligase (Ibl). The <jats:italic>p</jats:italic> -cymene-specific protein profile of “ <jats:named-content content-type="genus-species">Thauera</jats:named-content> ” sp. pCyN2, on the other hand, encompassed proteins homologous to subunits of toluene-activating benzylsuccinate synthase (termed [4-isopropylbenzyl]succinate synthase IbsABCDEF; identified subunits, IbsAE) and protein homologs of the benzylsuccinate β-oxidation (Bbs) pathway (termed BisABCDEFGH; all identified except for BisEF). This study reveals that two related denitrifying bacteria employ fundamentally different peripheral degradation routes for one and the same substrate, <jats:italic>p</jats:italic> -cymene, with the two pathways apparently converging at the level of 4-isopropylbenzoyl-CoA. </jats:p>
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