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

Journal Article (2017)
Author(s)

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 (TU Delft - BT/Biocatalysis)

Marco W. Fraaije (University Medical Center Groningen)

S. Kara (Hamburg University of Technology)

Research Group
BT/Biocatalysis
Copyright
© 2017 Lei Huang, Elvira Romero, Anna K. Ressmann, Florian Rudroff, F. Hollmann, Marco W. Fraaije, S. Kara
DOI related publication
https://doi.org/10.1002/adsc.201700401
More Info
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Publication Year
2017
Language
English
Copyright
© 2017 Lei Huang, Elvira Romero, Anna K. Ressmann, Florian Rudroff, F. Hollmann, Marco W. Fraaije, S. Kara
Research Group
BT/Biocatalysis
Issue number
12
Volume number
359
Pages (from-to)
2142-2148
Reuse Rights

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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.).

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