Unusual C=C bond isomerization of an α,β-unsaturated γ-butyrolactone catalysed by flavoproteins from the old yellow enzyme family.

Autor: Durchschein K; Organic & Bioorganic Chemistry, Department of Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz, Austria., Wallner S, Macheroux P, Zangger K, Fabian WM, Faber K
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2012 Nov 05; Vol. 13 (16), pp. 2346-51. Date of Electronic Publication: 2012 Sep 28.
DOI: 10.1002/cbic.201200475
Abstrakt: An unexpected, redox-neutral C=C bond isomerization of a γ-butyrolactone bearing an exo-methylene unit to the thermodynamically more favoured endo isomer (k(cat) =0.076 s(-1) ) catalysed by flavoproteins from the Old Yellow Enzyme family was discovered. Theoretical calculations and kinetic data support a mechanism through which the isomerization proceeds through FMN-mediated hydride addition onto exo-Cβ, followed by hydride abstraction from endo-Cβ', which is in line with the well-established C=C bond bioreduction of OYEs. This new isomerase activity enriches the catalytic versatility of ene-reductases.
(Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Databáze: MEDLINE
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