Grogan, Gideon James orcid.org/0000-0003-1383-7056, Hutton, Amy, Zhao, Fei et al. (7 more authors) (2025) An Engineered Biocatalyst for Enantioselective Hydrazone Reduction. Angewandte Chemie International Edition. e202424350. ISSN 1433-7851
Abstract
Enantioselective reduction of hydrazones provides a convergent and versatile route to synthesize hydrazine-containing motifs that are commonly found in pharmaceuticals and agrochemicals. However current methods require the use of precious metals, costly chiral ligands and/or forcing reaction conditions. Here, we report the development of a biocatalytic approach for enantioselective hydrazone reduction using engineered imine reductases. Following evaluation of an in-house panel of >400 IRED sequences, we identified a single IR361 I127F L179V variant that promotes reduction of Cbz-protected hydrazones. Introduction of an additional two mutations via directed evolution afforded HRED1.1 that is 20-fold more active than the parent template and promotes reduction of a variety of protected hydrazones in high yields and selectivities (>99% e.e.), including in preparative scale biotransformations. Structural analysis of HRED1.1 provides insights into the origins of its unique hydrazone reductase activity. This study offers a powerful biocatalytic route to synthesize valuable chiral hydrazine products and further expands the impressive range of transformations accessible with engineered imine reductases.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | This is an author-produced version of the published paper. Uploaded in accordance with the University’s Research Publications and Open Access policy. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 22 Apr 2025 13:30 |
Last Modified: | 12 May 2025 11:55 |
Published Version: | https://doi.org/10.1002/anie.202424350 |
Status: | Published online |
Refereed: | Yes |
Identification Number: | 10.1002/anie.202424350 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:225654 |