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

Katharina Durchschein, Silvia Wallner, Peter Macheroux, Klaus Zangger, Walter M F Fabian, Kurt Faber

Chembiochem : a European journal of chemical biology 2012 Nov 05

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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.

Citation

Katharina Durchschein, Silvia Wallner, Peter Macheroux, Klaus Zangger, Walter M F Fabian, Kurt Faber. Unusual C=C bond isomerization of an α,β-unsaturated γ-butyrolactone catalysed by flavoproteins from the old yellow enzyme family. Chembiochem : a European journal of chemical biology. 2012 Nov 05;13(16):2346-51