6:2 Fluorotelomer sulfonic acid (6:2 FTSA) is a dominant per- and poly-fluoroalkyl substance (PFAS) in aqueous film-forming foam (AFFF)-impacted soil. While its biotransformation mechanisms have been studied, the complex effects of plants, nutrients, and soil microbiome interactions on the fate and removal of 6:2 FTSA are poorly understood. This study systematically investigated the potential of phytoremediation for 6:2 FTSA by Arabidopsis thaliana coupled with bioaugmentation of Rhodococcus jostiiRHA1 (designated as RHA1 hereafter) under different nutrient and microbiome conditions. Hyperaccumulation of 6:2 FTSA, defined as tissue/soil concentration > 10 and high translocation factor > 3, was observed in plants. However, biotransformation of 6:2 FTSA only occurred under sulfur-limited conditions. Spiking RHA1 not only enhanced the biotransformation of 6:2 FTSA in soil but also promoted plant growth. Soil microbiome analysis uncovered Rhodococcus as one of the dominant species in all RHA1-spiked soil. Different nutrients such as sulfur and carbon, bioaugmentation, and amendment of 6:2 FTSA caused significant changes in - the microbial community structure. This study revealed the synergistic effects of phytoremediation and bioaugmentation on 6:2 FTSA removal. and highlighted that the fate of 6:2 FTSA was highly influenced by the complex interactions of plants, nutrients, and soil microbiome.
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Desulfonation and defluorination of 6:2 fluorotelomer sulfonic acid (6:2 FTSA) by Rhodococcus jostii RHA1: Carbon and sulfur sources, enzymes, and pathways
6:2 fluorotelomer sulfonic acid (6:2 FTSA) is one per- and poly-fluoroalkyl substances commonly detected in the environment. While biotransformation of 6:2 FTSA has been reported, factors affecting desulfonation and defluorination of 6:2 FTSA remain poorly understood. This study elucidated the effects of carbon and sulfur sources on the gene expression of Rhodococcus jostii RHA1 which is responsible for the 6:2 FTSA biotransformation. While alkane monooxygenase and cytochrome P450 were highly expressed in ethanol-, 1-butanol-, and n-octane-grown RHA1 in sulfur-rich medium, these cultures only defluorinated 6:2 fluorotelomer alcohol but not 6:2 FTSA, suggesting that the sulfonate group in 6:2 FTSA hinders enzymatic defluorination. In sulfur-free growth media, alkanesulfonate monooxygenase was linked to desulfonation of 6:2 FTSA; while alkane monooxygenase, haloacid dehalogenase, and cytochrome P450 were linked to defluorination of 6:2 FTSA. The desulfonation and defluorination ability of these enzymes toward 6:2 FTSA were validated through heterologous gene expression and in vitro assays. Four degradation metabolites were confirmed and one was identified as a tentative metabolite. The results provide a new understanding of 6:2 FTSA biotransformation by RHA1. The genes encoding these desulfonating- and defluorinating-enzymes are potential markers to be used to assess 6:2 FTSA biotransformation in the environment.
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- Award ID(s):
- 1914707
- NSF-PAR ID:
- 10344288
- Date Published:
- Journal Name:
- Journal of hazardous materials
- ISSN:
- 0304-3894
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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Abstract Fungal degradation of 6:2 fluorotelomer alcohol (6:2 FTOH, C6F13CH2CH2OH) by two wood‐decaying fungal strains and six fungal isolates from a site contaminated with per‐ and polyfluoroalkyl substances (PFASs) was investigated. 6:2 FTOH is increasingly being used in FTOH‐based products, and previous reports on the microbial fate of 6:2 FTOH have focused on bacteria and environmental microbial consortia. Prior to this study, one report demonstrated that the 6:2 FTOH biotransformation by the wood‐decaying fungus,
Phanerochaete chrysosporium , generated more polyfluoroalkyl substances, such as 5:3 acid (F(CF2)5CH2CH2COOH), and diverted away from producing the highly stable perfluorocarboxylic acids (PFCAs). Most of the fungi (Gloeophyllum trabeum and isolates TW4‐2, TW4‐1, B79, and B76) examined in this study showed similar degradation patterns, further demonstrating that fungi yield more 5:3 acid (up to 51 mol% of initial 6:2 FTOH dosed) relative to other metabolites (up to 12 mol% total PFCAs). However, medium amendments can potentially improve 6:2 FTOH biotransformation rates and product profiles. The six fungal isolates tolerated up to 100 or 1,000 milligrams per liter of perfluorooctanoic acid and perfluorooctane sulfonic acid, and some isolates experienced increased growth with increasing concentrations. This study proposes that fungal pathways must be considered for the biotransformation of potential PFAS precursors, such as 6:2 FTOH, and suggests the basis for selecting proper microorganisms for remediation of fluoroalkyl‐contaminated sites. -
Fluorochemicals are a widely distributed class of compounds and have been utilized across a wide range of industries for decades. Given the environmental toxicity and adverse health threats of some fluorochemicals, the development of new methods for their decomposition is significant to public health. However, the carbon–fluorine (C–F) bond is among the most chemically robust bonds; consequently, the degradation of fluorinated hydrocarbons is exceptionally difficult. Here, metalloenzymes that catalyze the cleavage of this chemically challenging bond are reviewed. These enzymes include histidine-ligated heme-dependent dehaloperoxidase and tyrosine hydroxylase, thiolate-ligated heme-dependent cytochrome P450, and four nonheme oxygenases, namely, tetrahydrobiopterin-dependent aromatic amino acid hydroxylase, 2-oxoglutarate-dependent hydroxylase, Rieske dioxygenase, and thiol dioxygenase. While much of the literature regarding the aforementioned enzymes highlights their ability to catalyze C–H bond activation and functionalization, in many cases, the C–F bond cleavage has been shown to occur on fluorinated substrates. A copper-dependent laccase-mediated system representing an unnatural radical defluorination approach is also described. Detailed discussions on the structure–function relationships and catalytic mechanisms provide insights into biocatalytic defluorination, which may inspire drug design considerations and environmental remediation of halogenated contaminants.more » « less
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Abstract Across insect genomes, the size of the cytochrome P450 monooxygenase (
CYP ) gene superfamily varies widely.CYP ome size variation has been attributed to reciprocal adaptive radiations in insect detoxification genes in response to plant biosynthetic gene radiations driven by co‐evolution between herbivores and their chemically defended hostplants. Alternatively, variation inCYP ome size may be due to random “birth‐and‐death” processes, whereby exponential increase via gene duplications is limited by random decay via gene death or transition via divergence. We examinedCYP ome diversification in the genomes of seven Lepidoptera species varying in host breadth from monophagous (Bombyx mori ) to highly polyphagous (Amyelois transitella ).CYP ome size largely reflects the size of Clan 3, the clan associated with xenobiotic detoxification, and to some extent phylogenetic age. Consistently across genomes, familiesCYP 6,CYP 9 andCYP 321 are most diverse andCYP 6AB ,CYP 6AE ,CYP 6B,CYP 9A andCYP 9G are most diverse among subfamilies. Higher gene number in subfamilies is due to duplications occurring primarily after speciation and specialization (“P450 blooms”), and the genes are arranged in clusters, indicative of active duplicating loci. In the parsnip webworm,Depressaria pastinacella , gene expression levels in large subfamilies are high relative to smaller subfamilies. Functional and phylogenetic data suggest a correlation between highly dynamic loci (reflective of extensive gene duplication, functionalization and in some cases loss) and the ability of enzymes encoded by these genes to metabolize hostplant defences, consistent with an adaptive, nonrandom process driven by ecological interactions. -
Abstract Fungal infection of grasses, including rice (Oryza sativa), sorghum (Sorghum bicolor), and barley (Hordeum vulgare), induces the formation and accumulation of flavonoid phytoalexins. In maize (Zea mays), however, investigators have emphasized benzoxazinoid and terpenoid phytoalexins, and comparatively little is known about flavonoid induction in response to pathogens. Here, we examined fungus-elicited flavonoid metabolism in maize and identified key biosynthetic enzymes involved in the formation of O-methylflavonoids. The predominant end products were identified as two tautomers of a 2-hydroxynaringenin-derived compound termed xilonenin, which significantly inhibited the growth of two maize pathogens, Fusarium graminearum and Fusarium verticillioides. Among the biosynthetic enzymes identified were two O-methyltransferases (OMTs), flavonoid OMT 2 (FOMT2), and FOMT4, which demonstrated distinct regiospecificity on a broad spectrum of flavonoid classes. In addition, a cytochrome P450 monooxygenase (CYP) in the CYP93G subfamily was found to serve as a flavanone 2-hydroxylase providing the substrate for FOMT2-catalyzed formation of xilonenin. In summary, maize produces a diverse blend of O-methylflavonoids with antifungal activity upon attack by a broad range of fungi.more » « less
- Free Publicly Accessible Full Text
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Accepted Manuscript1.0
- Journal Article:
- https://doi.org/10.1016/j.jhazmat.2021.127052
