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dc.contributor.authorHeeb, Norbert V.-
dc.contributor.authorWyss, Simon A.-
dc.contributor.authorGeueke, Birgit-
dc.contributor.authorFleischmann, Thomas-
dc.contributor.authorKohler, Hans-Peter E.-
dc.contributor.authorLienemann, Peter-
dc.date.accessioned2018-11-16T10:03:51Z-
dc.date.available2018-11-16T10:03:51Z-
dc.date.issued2014-
dc.identifier.issn0045-6535de_CH
dc.identifier.issn1879-1298de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/12902-
dc.description.abstractHexabromocyclododecanes (HBCDs) and hexachlorocyclohexanes (HCHs) are lipophilic, polyhalogenated hydrocarbons with comparable stereochemistry. Bacterial evolution in HCH-contaminated soils resulted in the development of several Spingomonadaceae which express a series of HCH-converting enzymes. We showed that LinB, a haloalkane dehalogenase from Sphingobium indicum B90A, also transforms various HBCDs besides HCHs. Here we present evidence that LinA2, another dehalogenase from S. indicum also converts certain HBCDs to pentabromocyclododecenes (PBCDEs). Racemic mixtures of α-, β-, γ-HBCDs, a mixture of them, and δ-HBCD, a meso form, were exposed to LinA2. Substantial conversion of (-)β-HBCD was observed, but all other stereoisomers were not transformed significantly. The enantiomeric excess (EE) of β-HBCDs increased up to 60% in 32 h, whereas EE values of α- and γ-HBCDs were not affected. Substrate conversion and product formation were described with second-order kinetic models. One major (P1β) and possibly two minor (P2β, P3β) metabolites were detected. Respective mass spectra showed the characteristic isotope pattern of PBCDEs, the HBr elimination products of HBCDs. Michaelis-Menten parameters KM=0.47 ± 0.07 μM and vmax=0.17 ± 0.01 μmoll(-1)h(-1) were deduced from exposure data with varying enzyme/substrate ratios. LinA2 is more substrate specific than LinB, the latter converted all tested HBCDs, LinA2 only one. The widespread HCH pollution favored the selection and evolution of bacteria converting these compounds. We found that LinA2 and LinB, two of these HCH-converting enzymes expressed in S. indicum B90A, also dehalogenate HBCDs to lower brominated compounds, indicating that structural similarities of both classes of compounds are recognized at the level of substrate-protein interactions.de_CH
dc.language.isoende_CH
dc.publisherElsevierde_CH
dc.relation.ispartofChemospherede_CH
dc.rightsLicence according to publishing contractde_CH
dc.subjectBrominated flame retardantsde_CH
dc.subjectHBCD biotransformationde_CH
dc.subjectHCH-converting bacterial enzymede_CH
dc.subjectLinA2 metabolitesde_CH
dc.subjectPersistent organic pollutantsde_CH
dc.subjectBiocatalysisde_CH
dc.subjectBiotransformationde_CH
dc.subjectBrominated hydrocarbonsde_CH
dc.subjectHydrolasesde_CH
dc.subjectKineticsde_CH
dc.subjectLindanede_CH
dc.subjectPolystyrenesde_CH
dc.subjectSoil pollutantsde_CH
dc.subjectSphingomonadaceaede_CH
dc.subjectStereoisomerismde_CH
dc.subjectHalogenationde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleLinA2, a HCH-converting bacterial enzyme that dehydrohalogenates HBCDsde_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.2013.12.035de_CH
dc.identifier.pmid24444415de_CH
zhaw.funding.euNode_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end202de_CH
zhaw.pages.start194de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume107de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
Appears in collections:Publikationen Life Sciences und Facility Management

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Heeb, N. V., Wyss, S. A., Geueke, B., Fleischmann, T., Kohler, H.-P. E., & Lienemann, P. (2014). LinA2, a HCH-converting bacterial enzyme that dehydrohalogenates HBCDs. Chemosphere, 107, 194–202. https://doi.org/10.1016/j.chemosphere.2013.12.035
Heeb, N.V. et al. (2014) ‘LinA2, a HCH-converting bacterial enzyme that dehydrohalogenates HBCDs’, Chemosphere, 107, pp. 194–202. Available at: https://doi.org/10.1016/j.chemosphere.2013.12.035.
N. V. Heeb, S. A. Wyss, B. Geueke, T. Fleischmann, H.-P. E. Kohler, and P. Lienemann, “LinA2, a HCH-converting bacterial enzyme that dehydrohalogenates HBCDs,” Chemosphere, vol. 107, pp. 194–202, 2014, doi: 10.1016/j.chemosphere.2013.12.035.
HEEB, Norbert V., Simon A. WYSS, Birgit GEUEKE, Thomas FLEISCHMANN, Hans-Peter E. KOHLER und Peter LIENEMANN, 2014. LinA2, a HCH-converting bacterial enzyme that dehydrohalogenates HBCDs. Chemosphere. 2014. Bd. 107, S. 194–202. DOI 10.1016/j.chemosphere.2013.12.035
Heeb, Norbert V., Simon A. Wyss, Birgit Geueke, Thomas Fleischmann, Hans-Peter E. Kohler, and Peter Lienemann. 2014. “LinA2, a HCH-Converting Bacterial Enzyme That Dehydrohalogenates HBCDs.” Chemosphere 107: 194–202. https://doi.org/10.1016/j.chemosphere.2013.12.035.
Heeb, Norbert V., et al. “LinA2, a HCH-Converting Bacterial Enzyme That Dehydrohalogenates HBCDs.” Chemosphere, vol. 107, 2014, pp. 194–202, https://doi.org/10.1016/j.chemosphere.2013.12.035.


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