Journal
ADVANCED SYNTHESIS & CATALYSIS
Volume 358, Issue 11, Pages 1810-1819Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.201600241
Keywords
alcohol dehydrogenases; biotransformations; cofactor regeneration; enzyme catalysis; NAD(P)H-oxidase
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Funding
- Fonds of the Chemical Industry
- Ministry of Innovation, Science and Research of the German federal state of North Rhine-Westphalia
- Heinrich Heine University Dusseldorf
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Enzymatic oxidations of primary and secondary alcohols catalysed by nicotinamide dependent alcohol dehydrogenases on the preparative scale require cofactor regeneration systems. Of critical value from an economic and ecological perspective is the application of NAD(P)H-oxidases, which utilise molecular oxygen as a cost-effective, atom-efficient and environmentally benign oxidant to regenerate the cofactor NAD(P)(+). Herein, the P450 BM3 monooxygenase from Bacillus megaterium is presented as an NAD(P)H-oxidase for the successful regeneration of both NADP(+) and NAD(+) on the preparative scale. This enzyme was exemplarily applied for ADH-catalysed oxidative kinetic resolutions of racemic secondary alcohols and the desymmetrisation of a meso-diol leading to enantiomerically enriched secondary alcohols in both cases. Furthermore, the ADH-catalysed oxidation of a primary alcohol targeting the corresponding aldehyde was performed. The obtained results significantly broaden the scope of feasible oxidative biotransformations, thereby increasing the number of synthetic reactions complying with key challenges of a modern and sustainable chemistry such as mild reaction conditions, environmentally benign solvents, and biodegradable non-toxic catalysts.
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