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Peroxygenase-Enabled Reductive Kinetic Resolution for the Enantioenrichment of Organoperoxides |
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| Authors: | Qianqian Shen Juzhang Yan Yuchen Han Prof. Dr. Zaoxiao Zhang Huanhuan Li Prof. Dr. Dulin Kong Prof. Dr. Jianjun Shi Prof. Dr. Chengsen Cui Prof. Dr. Wuyuan Zhang |
| Affiliation: | 1. Key Laboratory of Engineering Biology for Low-carbon Manufacturing Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West 7th Avenue, Tianjin, 300308 China School of Chemical Engineering and Technology, Xi'an Jiaotong University, Xi'an, 710049 China;2. Key Laboratory of Engineering Biology for Low-carbon Manufacturing Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West 7th Avenue, Tianjin, 300308 China;3. School of Chemical Engineering and Technology, Xi'an Jiaotong University, Xi'an, 710049 China;4. School of Pharmacy, Hainan Medical University, Haikou, 571199, Hainan China;5. College of Chemistry and Chemical Engineering, Hainan Normal University, Haikou, 571158, Hainan China |
| Abstract: | Enantiomerically pure organoperoxides serve as valuable precursors in organic transformations. Herein, we present the first examples of unspecific peroxygenase catalyzed kinetic resolution of racemic organoperoxides through asymmetric reduction. Through meticulous investigation of the reaction conditions, it is shown that the unspecific peroxygenase from Agrocybe aegerita (AaeUPO) exhibits robust catalytic activity in the kinetic resolution reactions of the model substrate with turnover numbers up to 60000 and turnover frequency of 5.6 s−1. Various aralkyl organoperoxides were successfully resolved by AaeUPO, achieving excellent enantioselectivities (e.g., up to 99 % ee for the (S)-organoperoxide products). Additionally, we screened commercial peroxygenase variants to obtain the organoperoxides with complementary chirality, with one mutant yielding the (R)-products. While unspecific peroxygenases have been extensively demonstrated as a powerful oxidative catalysts, this study highlights their usefulness in catalyzing the reduction of organoperoxides and providing versatile chiral synthons. |
| Keywords: | Biocatalysis Enzymatic reduction Kinetic resolution Organoperoxides Peroxygenase |