Yu, Kun and Zou, Zhi and Igareta, Nico V. and Tachibana, Ryo and Bechter, Julia and Köhler, Valentin and Chen, Dongping and Ward, Thomas R.. (2023) Artificial Metalloenzyme-Catalyzed Enantioselective Amidation via Nitrene Insertion in Unactivated C(sp³)–H Bonds. Journal of the American Chemical Society, 145 (30). pp. 16621-16629.
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Abstract
Enantioselective C–H amidation offers attractive means to assemble C–N bonds to synthesize high-added value, nitrogen-containing molecules. In recent decades, complementary enzymatic and homogeneous-catalytic strategies for C–H amidation have been reported. Herein, we report on an artificial metalloenzyme (ArM) resulting from anchoring a biotinylated Ir-complex within streptavidin (Sav). The resulting ArM catalyzes the enantioselective amidation of unactivated C(sp3)–H bonds. Chemogenetic optimization of the Ir cofactor and Sav led to significant improvement in both the activity and enantioselectivity. Up to >700 TON and 92% ee for the amidation of unactivated C(sp3)–H bonds was achieved. The single crystal X-ray analysis of the artificial nitrene insertase (ANIase) combined with quantum mechanics-molecular mechanics (QM-MM) calculations sheds light on critical second coordination sphere contacts leading to improved catalytic performance.
Faculties and Departments: | 05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward) |
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UniBasel Contributors: | Ward, Thomas R. R. |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | American Chemical Society |
ISSN: | 0002-7863 |
e-ISSN: | 1520-5126 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Language: | English |
Identification Number: |
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edoc DOI: | |
Last Modified: | 21 Sep 2023 14:42 |
Deposited On: | 21 Sep 2023 14:42 |
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