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The growth yield of Aminobacter niigataensis MSH1 on the micropollutant 2,6-Dichlorobenzamide decreases substantially at trace substrate concentrations
Raes, B., Wang, J., Horemans, B., Dirckx, L., Waldherr, S., Kohler, H. P. E., & Springael, D. (2023). The growth yield of Aminobacter niigataensis MSH1 on the micropollutant 2,6-Dichlorobenzamide decreases substantially at trace substrate concentrations. Environmental Science and Technology, 58, 2859-2869. https://doi.org/10.1021/acs.est.3c06883
Elucidating the role of O<sub>2</sub> uncoupling in the oxidative biodegradation of organic contaminants by Rieske non-heme iron dioxygenases
Bopp, C. E., Bernet, N. M., Kohler, H. P. E., & Hofstetter, T. B. (2022). Elucidating the role of O2 uncoupling in the oxidative biodegradation of organic contaminants by Rieske non-heme iron dioxygenases. ACS Environmental Au, 2(5), 428-440. https://doi.org/10.1021/acsenvironau.2c00023
Enzymatic synthesis and formation kinetics of mono- and di-hydroxylated chlorinated paraffins with the bacterial dehalogenase LinB from <em>Sphingobium indicum</em>
Knobloch, M. C., Mathis, F., Fleischmann, T., Kohler, H. P. E., Kern, S., Bleiner, D., & Heeb, N. V. (2022). Enzymatic synthesis and formation kinetics of mono- and di-hydroxylated chlorinated paraffins with the bacterial dehalogenase LinB from Sphingobium indicum. Chemosphere, 291, 132939 (10 pp.). https://doi.org/10.1016/j.chemosphere.2021.132939
Biodegradation of poly(butylene succinate) in soil laboratory incubations assessed by stable carbon isotope labelling
Nelson, T. F., Baumgartner, R., Jaggi, M., Bernasconi, S. M., Battagliarin, G., Sinkel, C., … Sander, M. (2022). Biodegradation of poly(butylene succinate) in soil laboratory incubations assessed by stable carbon isotope labelling. Nature Communications, 13(1), 5691 (16 pp.). https://doi.org/10.1038/s41467-022-33064-8
Substrate-specific coupling of O<sub>2</sub> activation to hydroxylations of aromatic compounds by rieske non-heme iron dioxygenases
Pati, S. G., Bopp, C. E., Kohler, H. P. E., & Hofstetter, T. B. (2022). Substrate-specific coupling of O2 activation to hydroxylations of aromatic compounds by rieske non-heme iron dioxygenases. ACS Catalysis, 12(11), 6444-6456. https://doi.org/10.1021/acscatal.2c00383
Transformation of ε-HBCD with the &lt;em&gt;Sphingobium Indicum&lt;/em&gt; enzymes LinA1, LinA2 and LinATM, a triple mutant of LinA2
Heeb, N. V., Hubeli, J., Fleischmann, T., Lienemann, P., Nayyar, N., Lal, R., & Kohler, H. P. E. (2021). Transformation of ε-HBCD with the Sphingobium Indicum enzymes LinA1, LinA2 and LinATM, a triple mutant of LinA2. Chemosphere, 267, 129217 (12 pp.). https://doi.org/10.1016/j.chemosphere.2020.129217
Transformation of short-chain chlorinated paraffins and olefins with the bacterial dehalogenase LinB from <em>Sphingobium Indicum</em> – Kinetic models for the homologue-specific conversion of reactive and persistent material
Knobloch, M. C., Schinkel, L., Kohler, H. P. E., Mathis, F., Kern, S., Bleiner, D., & Heeb, N. V. (2021). Transformation of short-chain chlorinated paraffins and olefins with the bacterial dehalogenase LinB from Sphingobium Indicum – Kinetic models for the homologue-specific conversion of reactive and persistent material. Chemosphere, 283, 131199 (12 pp.). https://doi.org/10.1016/j.chemosphere.2021.131199
Transformation of short-chain chlorinated paraffins by the bacterial haloalkane dehalogenase LinB – Formation of mono- and di-hydroxylated metabolites
Knobloch, M. C., Schinkel, L., Schilling, I., Kohler, H. P. E., Lienemann, P., Bleiner, D., & Heeb, N. V. (2021). Transformation of short-chain chlorinated paraffins by the bacterial haloalkane dehalogenase LinB – Formation of mono- and di-hydroxylated metabolites. Chemosphere, 262, 128288 (13 pp.). https://doi.org/10.1016/j.chemosphere.2020.128288
Enzyme kinetics of organic contaminant oxygenations
Bopp, C. E., Kohler, H. P. E., & Hofstetter, T. B. (2020). Enzyme kinetics of organic contaminant oxygenations. Chimia, 74(3), 108-114. https://doi.org/10.2533/chimia.2020.108
Photochemical transformation of poly(butylene adipate-<i>co</i>-terephthalate) and its effects on enzymatic hydrolyzability
De Hoe, G. X., Zumstein, M. T., Getzinger, G. J., Rüegsegger, I., Kohler, H. P. E., Maurer-Jones, M. A., … McNeill, K. (2019). Photochemical transformation of poly(butylene adipate-co-terephthalate) and its effects on enzymatic hydrolyzability. Environmental Science and Technology, 53(5), 2472-2481. https://doi.org/10.1021/acs.est.8b06458
Biotransformation of short-chain chlorinated paraffins (SCCPs) with LinA2: a HCH and HBCD converting bacterial dehydrohalogenase
Heeb, N. V., Schalles, S., Lehner, S., Schinkel, L., Schilling, I., Lienemann, P., … Kohler, H. P. E. (2019). Biotransformation of short-chain chlorinated paraffins (SCCPs) with LinA2: a HCH and HBCD converting bacterial dehydrohalogenase. Chemosphere, 226, 744-754. https://doi.org/10.1016/j.chemosphere.2019.03.169
Modelling carbofuran biotransformation by: <i>Novosphingobium</i> sp. KN65.2 in the presence of coincidental carbon and indigenous microbes
Liu, L., Helbling, D. E., Kohler, H. P. E., & Smets, B. F. (2019). Modelling carbofuran biotransformation by: Novosphingobium sp. KN65.2 in the presence of coincidental carbon and indigenous microbes. Environmental Science: Water Research and Technology, 5(4), 798-807. https://doi.org/10.1039/c8ew00929e
Quantification of synthetic polyesters from biodegradable mulch films in soils
Nelson, T. F., Remke, S. C., Kohler, H. P. E., McNeill, K., & Sander, M. (2019). Quantification of synthetic polyesters from biodegradable mulch films in soils. Environmental Science and Technology, 54(1), 266-275. https://doi.org/10.1021/acs.est.9b05863
&lt;em&gt;Aminobacter&lt;/em&gt; sp. MSH1 mineralises the groundwater micropollutant 2,6-dichlorobenzamide through a unique chlorobenzoate catabolic pathway.
Raes, B., Horemans, B., Rentsch, D., T'Syen, J., Ghequire, M. G. K., De Mot, R., … Springael, D. (2019). Aminobacter sp. MSH1 mineralises the groundwater micropollutant 2,6-dichlorobenzamide through a unique chlorobenzoate catabolic pathway. Environmental Science and Technology, 53(17), 10146-10156. https://doi.org/10.1021/acs.est.9b02021
Assessing the environmental transformation of nanoplastic through <sup>13</sup>C-labelled polymers
Sander, M., Kohler, H. P. E., & McNeill, K. (2019). Assessing the environmental transformation of nanoplastic through 13C-labelled polymers. Nature Nanotechnology, 14(4), 301-303. https://doi.org/10.1038/s41565-019-0420-3
Assessing aerobic biotransformation of hexachlorocyclohexane isomers by compound-specific isotope analysis
Schilling, I. E., Bopp, C. E., Lal, R., Kohler, H. P. E., & Hofstetter, T. B. (2019). Assessing aerobic biotransformation of hexachlorocyclohexane isomers by compound-specific isotope analysis. Environmental Science and Technology, 53(13), 7419-7431. https://doi.org/10.1021/acs.est.9b01007
Kinetic isotope effects of the enzymatic transformation of <i>γ</i>-hexachlorocyclohexane by the lindane dehydrochlorinase variants LinA1 and LinA2
Schilling, I. E., Hess, R., Bolotin, J., Lal, R., Hofstetter, T. B., & Kohler, H. P. E. (2019). Kinetic isotope effects of the enzymatic transformation of γ-hexachlorocyclohexane by the lindane dehydrochlorinase variants LinA1 and LinA2. Environmental Science and Technology, 53(5), 2353-2363. https://doi.org/10.1021/acs.est.8b04234
Dos and do nots when assessing the biodegradation of plastics
Zumstein, M. T., Narayan, R., Kohler, H. P. E., McNeill, K., & Sander, M. (2019). Dos and do nots when assessing the biodegradation of plastics. Environmental Science and Technology, 53(17), 9967-9969. https://doi.org/10.1021/acs.est.9b04513
Ion trapping of amines in protozoa: a novel removal mechanism for micropollutants in activated sludge
Gulde, R., Anliker, S., Kohler, H. P. E., & Fenner, K. (2018). Ion trapping of amines in protozoa: a novel removal mechanism for micropollutants in activated sludge. Environmental Science and Technology, 52(1), 52-60. https://doi.org/10.1021/acs.est.7b03556
Kinetics and stereochemistry of LinB-catalyzed δ-HBCD transformation: comparison of <i>in vitro</i> and <i>in silico</i> results
Heeb, N. V., Mazenauer, M., Wyss, S., Geueke, B., Kohler, H. P. E., & Lienemann, P. (2018). Kinetics and stereochemistry of LinB-catalyzed δ-HBCD transformation: comparison of in vitro and in silico results. Chemosphere, 207, 118-129. https://doi.org/10.1016/j.chemosphere.2018.05.057
 

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