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dc.contributor.authorHeeb, Norbert V.-
dc.contributor.authorMazenauer, Manuel-
dc.contributor.authorWyss, Simon-
dc.contributor.authorGeueke, Birgit-
dc.contributor.authorKohler, Hans-Peter E.-
dc.contributor.authorLienemann, Peter-
dc.date.accessioned2023-07-20T12:33:59Z-
dc.date.available2023-07-20T12:33:59Z-
dc.date.issued2018-
dc.identifier.issn0045-6535de_CH
dc.identifier.issn1879-1298de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/28259-
dc.description.abstractLinB is a haloalkane dehalogenase found in Sphingobium indicum B90A, an aerobic bacterium isolated from contaminated soils of hexachlorocyclohexane (HCH) dumpsites. We showed that this enzyme also converts hexabromocyclododecanes (HBCDs). Here we give new insights in the kinetics and stereochemistry of the enzymatic transformation of δ-HBCD, which resulted in the formation of two pentabromocyclododecanols (PBCDols) as first- (P1δ, P2δ) and two tetrabromocyclododecadiols (TBCDdiols) as second-generation products (T1δ, T2δ). Enzymatic transformations of δ-HBCD, α1-PBCDol, one of the transformation products, and α2-PBCDol, its enantiomer, were studied and modeled with Michaelis-Menten (MM) kinetics. Respective MM-parameters KM, vmax, kcat/KM indicated that δ-HBCD is the best LinB substrate followed by α2- and α1-PBCDol. The stereochemistry of these transformations was modeled in silico, investigating respective enzyme-substrate (ES) and enzyme-product (EP) complexes. One of the four predicted ES-complexes led to the PBCDol product P1δ, identical to α2-PBCDol with the 1R,2R,5S,6R,9R,10S-configuration. An SN2-like substitution of bromine at C6 of δ-HBCD by Asp-108 of LinB and subsequent hydrolysis of the alkyl-enzyme led to α2-PBCDol. Modeling results further indicate that backside attacks at C1, C9 and C10 are reasonable too, selectively binding leaving bromide ions in a halide pocket found in LinB. Docking with α2-PBCDol, also allowed productive enzyme binding. A TBCD-1,5-diol with the 1S,2S,5R,6R,9S,10R-configuration is the predicted second-generation product T1δ. In conclusion, in vitro- and in silico findings now allow a detailed description of step-wise enzymatic dehalohydroxylation reactions of δ-HBCD to specific PBCDols and TBCDdiols at Å-resolution and predictions of their stereochemistry.de_CH
dc.language.isoende_CH
dc.publisherElsevierde_CH
dc.relation.ispartofChemospherede_CH
dc.rightsLicence according to publishing contractde_CH
dc.subjectHBCD biotransformationde_CH
dc.subjectHCH-converting bacterial enzyme LinBde_CH
dc.subjectMichaelis-menten kineticsde_CH
dc.subjectMolecular dockingde_CH
dc.subjectSphingomonadaceade_CH
dc.subjectStructure predictionde_CH
dc.subjectCatalysisde_CH
dc.subjectComputer Simulationde_CH
dc.subjectHydrocarbons, brominatedde_CH
dc.subjectKineticsde_CH
dc.subjectStereoisomerismde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleKinetics and stereochemistry of LinB-catalyzed δ-HBCD transformation : comparison of in vitro and in silico resultsde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.1016/j.chemosphere.2018.05.057de_CH
dc.identifier.pmid29793023de_CH
zhaw.funding.euNode_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end129de_CH
zhaw.pages.start118de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume207de_CH
zhaw.publication.reviewNot specifiedde_CH
zhaw.author.additionalNode_CH
zhaw.display.portraitYesde_CH
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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
Heeb, N.V. et al. (2018) ‘Kinetics and stereochemistry of LinB-catalyzed δ-HBCD transformation : comparison of in vitro and in silico results’, Chemosphere, 207, pp. 118–129. Available at: https://doi.org/10.1016/j.chemosphere.2018.05.057.
N. V. Heeb, M. Mazenauer, S. Wyss, B. Geueke, H.-P. E. Kohler, and P. Lienemann, “Kinetics and stereochemistry of LinB-catalyzed δ-HBCD transformation : comparison of in vitro and in silico results,” Chemosphere, vol. 207, pp. 118–129, 2018, doi: 10.1016/j.chemosphere.2018.05.057.
HEEB, Norbert V., Manuel MAZENAUER, Simon WYSS, Birgit GEUEKE, Hans-Peter E. KOHLER und Peter LIENEMANN, 2018. Kinetics and stereochemistry of LinB-catalyzed δ-HBCD transformation : comparison of in vitro and in silico results. Chemosphere. 2018. Bd. 207, S. 118–129. DOI 10.1016/j.chemosphere.2018.05.057
Heeb, Norbert V., Manuel Mazenauer, Simon Wyss, Birgit Geueke, Hans-Peter E. Kohler, and Peter Lienemann. 2018. “Kinetics and Stereochemistry of LinB-Catalyzed δ-HBCD Transformation : Comparison of in Vitro and in Silico Results.” Chemosphere 207: 118–29. https://doi.org/10.1016/j.chemosphere.2018.05.057.
Heeb, Norbert V., et al. “Kinetics and Stereochemistry of LinB-Catalyzed δ-HBCD Transformation : Comparison of in Vitro and in Silico Results.” Chemosphere, vol. 207, 2018, pp. 118–29, https://doi.org/10.1016/j.chemosphere.2018.05.057.


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