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Unusual CC Bond Isomerization of an α,β‐Unsaturated γ‐Butyrolactone Catalysed by Flavoproteins from the Old Yellow Enzyme Family
Author(s) -
Durchschein Katharina,
Wallner Silvia,
Macheroux Peter,
Zangger Klaus,
Fabian Walter M. F.,
Faber Kurt
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200475
Subject(s) - isomerization , flavoprotein , chemistry , enzyme , stereochemistry , double bond , biochemistry , organic chemistry , catalysis
An unexpected, redox‐neutral CC 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 CC bond bioreduction of OYEs. This new isomerase activity enriches the catalytic versatility of ene‐reductases.