Print Email Facebook Twitter Synthetic biomimetic coenzymes and alcohol dehydrogenases for asymmetric catalysis Title Synthetic biomimetic coenzymes and alcohol dehydrogenases for asymmetric catalysis Author Josa-Culleré, Laia (University of Oxford; Student TU Delft) Lahdenperä, Antti S.K. (University of Oxford; Student TU Delft) Ribaucourt, Aubert (University of Oxford; Student TU Delft) Höfler, G.T. (TU Delft BT/Biocatalysis) Gargiulo, S. (Student TU Delft) Liu, Yuan Yang (East China University of Science and Technology) Paradisi, Francesca (University of Nottingham) Hollmann, F. (TU Delft BT/Biocatalysis) Paul, C.E. (TU Delft BT/Biocatalysis) Date 2019 Abstract Redox reactions catalyzed by highly selective nicotinamide-dependent oxidoreductases are rising to prominence in industry. The cost of nicotinamide adenine dinucleotide coenzymes has led to the use of well-established elaborate regeneration systems and more recently alternative synthetic biomimetic cofactors. These biomimetics are highly attractive to use with ketoreductases for asymmetric catalysis. In this work, we show that the commonly studied cofactor analogue 1-benzyl-1,4-dihydronicotinamide (BNAH) can be used with alcohol dehydrogenases (ADHs) under certain conditions. First, we carried out the rhodium-catalyzed recycling of BNAH with horse liver ADH (HLADH), observing enantioenriched product only with unpurified enzyme. Then, a series of cell-free extracts and purified ketoreductases were screened with BNAH. The use of unpurified enzyme led to product formation, whereas upon dialysis or further purification no product was observed. Several other biomimetics were screened with various ADHs and showed no or very low activity, but also no inhibition. BNAH as a hydride source was shown to directly reduce nicotinamide adenine dinucleotide (NAD) to NADH. A formate dehydrogenase could also mediate the reduction of NAD from BNAH. BNAH was established to show no or very low activity with ADHs and could be used as a hydride donor to recycle NADH. Subject Alcohol dehydrogenasesCofactor regenerationFormate dehydrogenaseNicotinamide coenzyme biomimeticsRhodium catalyst To reference this document use: http://resolver.tudelft.nl/uuid:bdcbe467-8f92-4d21-b3f7-aa5751b51c33 DOI https://doi.org/10.3390/catal9030207 ISSN 2073-4344 Source Catalysts, 9 (3) Part of collection Institutional Repository Document type journal article Rights © 2019 Laia Josa-Culleré, Antti S.K. Lahdenperä, Aubert Ribaucourt, G.T. Höfler, S. Gargiulo, Yuan Yang Liu, Francesca Paradisi, F. Hollmann, C.E. Paul, More Authors Files PDF catalysts_09_00207.pdf 997.56 KB Close viewer /islandora/object/uuid:bdcbe467-8f92-4d21-b3f7-aa5751b51c33/datastream/OBJ/view