biostudies-literatureUnknown10(29)Yu YEnzymatic cleavage of C─F bonds in per- and polyfluoroalkyl substances (PFAS) is largely unknown but avidly sought to promote systems biology for PFAS bioremediation. Here, we report the reductive defluorination of α, β-unsaturated per- and polyfluorocarboxylic acids by <i>Acetobacterium</i> spp. The microbial defluorination products were structurally confirmed and showed regiospecificity and stereospecificity, consistent with their formation by enzymatic reactions. A comparison of defluorination activities among several <i>Acetobacterium</i> species indicated that a functional fluoride exporter was required for the detoxification of the released fluoride. Results from both in vivo inhibition tests and in silico enzyme modeling suggested the involvement of enzymes of the flavin-based electron-bifurcating caffeate reduction pathway [caffeoyl-CoA reductase (CarABCDE)] in the reductive defluorination. This is a report on specific microorganisms carrying out enzymatic reductive defluorination of PFAS, which could be linked to electron-bifurcating reductases that are environmentally widespread.Science advanceseado2957https://www.ebi.ac.uk/biostudies/studies/S-EPMC466959biostudies-literatureElectron bifurcation and fluoride efflux systems implicated in defluorination of perfluorinated unsaturated carboxylic acids by <i>Acetobacterium</i> spp.PMC466959Thoma CRichman JEChe SMen YJin BZhu YXing YWackett LZhao WXu FYu YfalseElectron bifurcation and fluoride efflux systems implicated in defluorination of perfluorinated unsaturated carboxylic acids by <i>Acetobacterium</i> spp.Enzymatic cleavage of C─F bonds in per- and polyfluoroalkyl substances (PFAS) is largely unknown but avidly sought to promote systems biology for PFAS bioremediation. Here, we report the reductive defluorination of α, β-unsaturated per- and polyfluorocarboxylic acids by <i>Acetobacterium</i> spp. The microbial defluorination products were structurally confirmed and showed regiospecificity and stereospecificity, consistent with their formation by enzymatic reactions. A comparison of defluorination activities among several <i>Acetobacterium</i> species indicated that a functional fluoride exporter was required for the detoxification of the released fluoride. Results from both in vivo inhibition tests and in silico enzyme modeling suggested the involvement of enzymes of the flavin-based electron-bifurcating caffeate reduction pathway [caffeoyl-CoA reductase (CarABCDE)] in the reductive defluorination. This is a report on specific microorganisms carrying out enzymatic reductive defluorination of PFAS, which could be linked to electron-bifurcating reductases that are environmentally widespread.2024-01-01T00:00:00Z2024 Jul2024-12-03T20:13:41.181Z2024-12-03T20:13:41.181ZS-EPMC4669593901840710.1126/sciadv.ado2957