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Open AccessCommunication

Enantioselective Epoxidation by Flavoprotein Monooxygenases Supported by Organic Solvents

1
Microbial Biotechnology, Faculty of Biology and Biotechnology, Ruhr-Universität Bochum, Universitätsstr. 150, 44780 Bochum, Germany
2
Activation of Small Molecules, Faculty of Chemistry and Biochemistry, Ruhr-Universität Bochum, Universitätsstr 150, 44780 Bochum, Germany
3
Fraunhofer UMSICHT, Division of Energy, Osterfelder Strasse 3, 46047 Oberhausen, Germany
*
Author to whom correspondence should be addressed.
Catalysts 2020, 10(5), 568; https://doi.org/10.3390/catal10050568
Received: 29 April 2020 / Revised: 14 May 2020 / Accepted: 14 May 2020 / Published: 19 May 2020
(This article belongs to the Special Issue Biocatalytic Process Optimization)
Styrene and indole monooxygenases (SMO and IMO) are two-component flavoprotein monooxygenases composed of a nicotinamide adenine dinucleotide (NADH)-dependent flavin adenine dinucleotide (FAD)-reductase (StyB or IndB) and a monooxygenase (StyA or IndA). The latter uses reduced FAD to activate oxygen and to oxygenate the substrate while releasing water. We circumvented the need for the reductase by direct FAD reduction in solution using the NAD(P)H-mimic 1-benzyl-1,4-dihydronicotinamide (BNAH) to fuel monooxygenases without NADH requirement. Herein, we report on the hitherto unknown solvent tolerance for the indole monooxygenase from Gemmobacter nectariphilus DSM15620 (GnIndA) and the styrene monooxygenase from Gordonia rubripertincta CWB2 (GrStyA). These enzymes were shown to convert bulky and rather hydrophobic styrene derivatives in the presence of organic cosolvents. Subsequently, BNAH-driven biotransformation was furthermore optimized with regard to the applied cosolvent and its concentration as well as FAD and BNAH concentration. We herein demonstrate that GnIndA and GrStyA enable selective epoxidations of allylic double bonds (up to 217 mU mg−1) in the presence of organic solvents such as tetrahydrofuran, acetonitrile, or several alcohols. Notably, GnIndA was found to resist methanol concentrations up to 25 vol.%. Furthermore, a diverse substrate preference was determined for both enzymes, making their distinct use very interesting. In general, our results seem representative for many IMOs as was corroborated by in silico mutagenetic studies. View Full-Text
Keywords: styrene monooxygenase; indole monooxygenase; two-component system; chiral biocatalyst; solvent tolerance; biotransformation; epoxidation; NAD(P)H-mimics styrene monooxygenase; indole monooxygenase; two-component system; chiral biocatalyst; solvent tolerance; biotransformation; epoxidation; NAD(P)H-mimics
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MDPI and ACS Style

Eggerichs, D.; Mügge, C.; Mayweg, J.; Apfel, U.-P.; Tischler, D. Enantioselective Epoxidation by Flavoprotein Monooxygenases Supported by Organic Solvents. Catalysts 2020, 10, 568.

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