Unknown

Dataset Information

0

A Simple Access to γ- and ε-Keto Arenes via Enzymatic Divergent C─H Bond Oxyfunctionalization.


ABSTRACT: Performing divergent C─H bond functionalization on molecules with multiple reaction sites is a significant challenge in organic chemistry. Biocatalytic oxyfunctionalization reactions of these compounds to the corresponding ketones/aldehydes are typically hindered by selectivity issues. To address these challenges, the catalytic performance of oxidoreductases is explored. The results show that combining the peroxygenase-catalyzed propargylic C─H bond oxidation with the Old Yellow Enzyme-catalyzed reduction of conjugated C─C triple bonds in one-pot enables the regio- and chemoselective oxyfunctionalization of sp3 C─H bonds that are distant from benzylic sites. This enzymatic approach yielded a variety of γ-keto arenes with diverse structural and electronic properties in yields of up to 99% and regioselectivity of 100%, which are difficult to achieve using other chemocatalysis and enzymes. By adjusting the C─C triple bond, the carbonyl group's position can be further tuned to yield ε-keto arenes. This enzymatic approach can be combined with other biocatalysts to establish new synthetic pathways for accessing various challenging divergent C─H bond functionalization reactions.

SUBMITTER: Li H 

PROVIDER: S-EPMC10700168 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

A Simple Access to γ- and ε-Keto Arenes via Enzymatic Divergent C─H Bond Oxyfunctionalization.

Li Huanhuan H   Zhang Yalan Y   Huang Yawen Y   Duan Peigao P   Ge Ran R   Han Xiaofeng X   Zhang Wuyuan W  

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 20231023 34


Performing divergent C─H bond functionalization on molecules with multiple reaction sites is a significant challenge in organic chemistry. Biocatalytic oxyfunctionalization reactions of these compounds to the corresponding ketones/aldehydes are typically hindered by selectivity issues. To address these challenges, the catalytic performance of oxidoreductases is explored. The results show that combining the peroxygenase-catalyzed propargylic C─H bond oxidation with the Old Yellow Enzyme-catalyzed  ...[more]

Similar Datasets

| S-EPMC9243031 | biostudies-literature
| S-EPMC10370552 | biostudies-literature
| S-EPMC11744798 | biostudies-literature
| S-EPMC11731486 | biostudies-literature
| S-EPMC5574032 | biostudies-literature
| S-EPMC5625593 | biostudies-literature
2025-02-17 | PXD059654 | Pride
| S-EPMC5947535 | biostudies-literature
| S-EPMC5952311 | biostudies-literature
| S-EPMC11650718 | biostudies-literature