France, Scott P., Aleku, Godwin A, Sharma, Mahima orcid.org/0000-0003-3960-2212 et al. (10 more authors) (2017) Biocatalytic Routes to Enantiomerically Enriched Dibenz[c,e]azepines. Angewandte Chemie International Edition. pp. 15589-15593. ISSN 1433-7851
Abstract
Biocatalytic retrosynthetic analysis of dibenz[c,e]azepines has highlighted the use of imine reductase (IRED) and ω-transaminase (ω-TA) biocatalysts to establish the key stereocentres of these molecules. Several enantiocomplementary IREDs were identified for the synthesis of (R)- and (S)-5-methyl-6,7-dihydro-5H-dibenz[c,e]azepine with excellent enantioselectivity, by reduction of the parent imines. Crystallographic evidence suggests that IREDs may be able to bind one conformer of the imine substrate such that, upon reduction, the major product conformer is generated directly. ω-TA biocatalysts were also successfully employed for the production of enantiopure 1-(2-bromophenyl)ethan-1-amine, thus enabling an orthogonal route for the installation of chirality into dibenz[c,e]azepine framework.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details |
Keywords: | biocatalysis,heterocycles,reductases,synthetic methods,transaminases |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) The University of York > Faculty of Sciences (York) > Psychology (York) > York Neuroimaging Centre |
Depositing User: | Pure (York) |
Date Deposited: | 10 Nov 2017 14:20 |
Last Modified: | 08 Feb 2025 00:25 |
Published Version: | https://doi.org/10.1002/anie.201708453 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1002/anie.201708453 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:123887 |