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Native hydrogenases use Earth\u2010abundant metals, but these cannot be applied for organic synthesis due, in part, to their substrate specificity. Herein, we report the design and development of manganese transfer hydrogenases based on the biotin\u2010streptavidin technology. By incorporating bio\u2010mimetic Mn(I) complexes into the binding cavity of streptavidin, and through chemo\u2010genetic optimization, we have obtained artificial enzymes that hydrogenate ketones with nearly quantitative yield and up to 98\u2009% enantiomeric excess (ee). These enzymes exhibit broad substrate scope and high functional\u2010group tolerance. According to QM\/MM calculations and X\u2010ray crystallography, the S112Y mutation, combined with the appropriate chemical structure of the Mn cofactor plays a critical role in the reactivity and enantioselectivity of the artificial metalloenzyme (ArMs). Our work highlights the potential of ArMs incorporating base\u2010meal cofactors for enantioselective organic synthesis.<\/jats:p>","DOI":"10.1002\/anie.202311896","type":"journal-article","created":{"date-parts":[[2023,9,6]],"date-time":"2023-09-06T04:57:51Z","timestamp":1693976271000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Manganese Transfer Hydrogenases Based on the Biotin\u2010Streptavidin Technology"],"prefix":"10.1002","volume":"62","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3080-1365","authenticated-orcid":false,"given":"Weijin","family":"Wang","sequence":"first","affiliation":[{"name":"Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering \u00c9cole Polytechnique F\u00e9d\u00e9rale de Lausanne ISIC-LSCI, BCH 3305  1015 Lausanne 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