{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Aukema KG"],"funding":["University of Minnesota","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["5202-5216"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9828342"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(11)"],"pubmed_abstract":["The present study examined the regulatory and metabolic response of the aromatic degrader Pseudomonas putida F1 and its tod operon, controlling toluene degradation, to fluorinated aromatic and aliphatic compounds. The tod operon is upregulated by inducer binding to the TodS sensing domain of a two-component regulator. The induced enzymes include toluene dioxygenase that initiates catabolic assimilation of benzenoid hydrocarbons. Toluene dioxygenase was shown to oxidize 6-fluoroindole to a meta-stable fluorescent product, 6-fluoroindoxyl. The fluorescent output allowed monitoring relative levels of tod operon induction in whole cells using microtiter well plates. Mono- and polyfluorinated aromatic compounds were shown to induce toluene dioxygenase, in some cases to a greater extent than com"],"journal":["Environmental microbiology"],"pubmed_title":["Fluoro-recognition: New in vivo fluorescent assay for toluene dioxygenase probing induction by and metabolism of polyfluorinated compounds."],"pmcid":["PMC9828342"],"funding_grant_id":["5T32GM008347‐27","T32 GM008347"],"pubmed_authors":["Aukema KG","Richman JE","Wackett LP","Tassoulas LJ","Bygd MD"],"additional_accession":[]},"is_claimable":false,"name":"Fluoro-recognition: New in vivo fluorescent assay for toluene dioxygenase probing induction by and metabolism of polyfluorinated compounds.","description":"The present study examined the regulatory and metabolic response of the aromatic degrader Pseudomonas putida F1 and its tod operon, controlling toluene degradation, to fluorinated aromatic and aliphatic compounds. The tod operon is upregulated by inducer binding to the TodS sensing domain of a two-component regulator. The induced enzymes include toluene dioxygenase that initiates catabolic assimilation of benzenoid hydrocarbons. Toluene dioxygenase was shown to oxidize 6-fluoroindole to a meta-stable fluorescent product, 6-fluoroindoxyl. The fluorescent output allowed monitoring relative levels of tod operon induction in whole cells using microtiter well plates. Mono- and polyfluorinated aromatic compounds were shown to induce toluene dioxygenase, in some cases to a greater extent than com","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-29T03:46:05.129Z","creation":"2024-11-20T14:28:42.493Z"},"accession":"S-EPMC9828342","cross_references":{"pubmed":["36054238"],"doi":["10.1111/1462-2920.16187"]}}