Intramolecular Benzoin Reaction Catalyzed by Benzaldehyde Lyase from Pseudomonas Fluorescens Biovar I

Angewandte Chemie - International Edition

5 years ago

Intramolecular Benzoin Reaction Catalyzed by Benzaldehyde Lyase from Pseudomonas Fluorescens Biovar I

Teodor Parella, Karel Hernández, Jesús Joglar, Pere Clapés, Claudia M. Wandtke, Giovanna Petrillo, Jordi Bujons, Isabel Usón

Intramolecular benzoin reactions catalyzed by benzaldehyde lyase from Pseudomonas fluorescens biovar I (BAL) are reported. The structure of the substrates envisaged for this reaction consists of two benzaldehyde derivatives linked by an alkyl chain. The structural requirements needed to achieve the intramolecular carbon–carbon bond reaction catalyzed by BAL were established. Thus, a linker consisting of a linear alkyl chain of three carbon atoms connected through ether-type bonds to the 2 and 2′ positions of two benzaldehyde moieties, which could be substituted with either Cl, Br, or OCH3 at either the 3 and 3′ or 5 and 5′ positions, were suitable substrates for BAL. Reactions with 61–84 % yields of the intramolecular product and ee values between 64 and 98 %, were achieved. Let's play BAL(L): Benzaldehyde lyase from Pseudomonas fluorescens biovar I (BAL) can catalyze enantioselective intramolecular benzoin reactions. The structural requirements for the substrate include two benzaldehyde moieties, with or without additional substituents at the 3,3′ and 5,5′ positions of the rings, connected by ether bonds to a C3 linker at the 2,2′ positions. The synthesis of non-natural macrocycles is now possible through this biocatalytic route.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201702278