LinA2, a HCH-converting bacterial enzyme that dehydrohalogenates HBCDs

Heeb, Norbert V.; Wyss, Simon A.; Geueke, Birgit; Fleischmann, Thomas; Kohler, Hans-Peter E.; Lienemann, Peter

doi:10.1016/j.chemosphere.2013.12.035

Publication type:	Article in scientific journal
Type of review:	Peer review (publication)
Title:	LinA2, a HCH-converting bacterial enzyme that dehydrohalogenates HBCDs
Authors:	Heeb, Norbert V. Wyss, Simon A. Geueke, Birgit Fleischmann, Thomas Kohler, Hans-Peter E. Lienemann, Peter
DOI:	10.1016/j.chemosphere.2013.12.035
Published in:	Chemosphere
Volume(Issue):	107
Page(s):	194
Pages to:	202
Issue Date:	2014
Publisher / Ed. Institution:	Elsevier
ISSN:	0045-6535 1879-1298
Language:	English
Subjects:	Brominated flame retardants; HBCD biotransformation; HCH-converting bacterial enzyme; LinA2 metabolites; Persistent organic pollutants; Biocatalysis; Biotransformation; Brominated hydrocarbons; Hydrolases; Kinetics; Lindane; Polystyrenes; Soil pollutants; Sphingomonadaceae; Stereoisomerism; Halogenation
Subject (DDC):	572: Biochemistry
Abstract:	Hexabromocyclododecanes (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.
URI:	https://digitalcollection.zhaw.ch/handle/11475/12902
Fulltext version:	Published version
License (according to publishing contract):	Licence according to publishing contract
Departement:	Life Sciences and Facility Management
Organisational Unit:	Institute of Chemistry and Biotechnology (ICBT)
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.