Nicotinamide Adenine Dinucleotide-Dependent Redox-Neutral Convergent Cascade for Lactonizations with Type II Flavin-Containing Monooxygenase

Journal article (2017)

Authors

Lei Huang Hamburg University of Technology
Elvira Romero University Medical Center Groningen
Anna K. Ressmann Technische Universität Wien
Florian Rudroff Technische Universität Wien
F. Hollmann BT/Biocatalysis - AS
Marco W. Fraaije University Medical Center Groningen
S. Kara Hamburg University of Technology
Research Group
BT/Biocatalysis (AS) (TU Delft)
Copyright: © 2017 Lei Huang, Elvira Romero, Anna K. Ressmann, Florian Rudroff, F. Hollmann, Marco W. Fraaije, S. Kara
DOI
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https://doi.org/10.1002/adsc.201700401
Biocatalysis Alcohol Dehydrogenase Baeyer-Villiger Monooxygenase Cofactor Specificity Redox-neutral Cascade
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Published Date

19-06-2017

Language

English

Reuse Rights

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Faculty

Applied Sciences

Department

BT/Biotechnologie

Research Group

BT/Biocatalysis

Abstract

A nicotinamide adenine dinucleotide (NADH)-dependent redox-neutral convergent cascade composed of a recently discovered type II flavin-containing monooxygenase (FMO−E) and horse liver alcohol dehydrogenase (HLADH) has been established. Two model reaction cascades were analyzed for the synthesis of γ-butyrolactone and chiral bicyclic lactones. In the former cascade, all substrates were converted into one single product γ-butyrolactone with high atom efficiency. More than 130 mM γ-butyrolactone were obtained when applying 100 mM cyclobutanone and 50 mM 1,4-butanediol in this cascade. In the second cascade where bicyclo[4.2.0]octan-7-one and cis-1,2-cyclohexanedimethanol were coupled, the ketone substrate was converted to the corresponding normal lactone with an ee value of 89–74% (3aS, 7aS) by FMO−E alone and the abnormal lactone with an ee value of >99% (3aR, 7aS) was formed by both HLADH and FMO−E. (Figure presented.).