Glucose Induces Heme Leakage and Suppresses H2O2 Uptake of Chloroperoxidase in the Asymmetric Hydroxylation of Ethylbenzene. Issue 12 (16th May 2022)

• Record Type: Journal Article
• Authors: Wang, Zheyu; Fu, Zhongwang; Jian, Yupei; Han, Yilei; Xia, Meng; Zhang, Shuiwei; Yan, Binhang; Jiang, Guoqiang; Lu, Diannan; Wu, Jianzhong; Liu, Zheng
• Is Part Of: ChemCatChem. Volume 14:Issue 12(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-05-16
• Subjects: Glucose -- peroxidase cascades -- chloroperoxidase -- direct functionalization of C−H bonds; Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.202200309
• Languages: English
• ISSNs: 1867-3880

Abstract

Abstract: As a basic feedstock for both natural life and chemical production, glucose is converted into various chemicals upon the help of peroxidase cascades composed of glucose oxidase (GOx) and peroxidases. However, little is known about the glucose effect on the structure and activity of peroxidases in a non‐natural environment. We report herein that glucose deactivates chloroperoxidase (CPO) used in the asymmetric hydroxylation of ethylbenzene into ( R )‐1‐phenylethanol. Through both experiment and molecular simulation, we discover that glucose deactivates CPO through hydrophobic interaction with heme and hydrogen bonding with Glu 183 . These interactions lead to heme leakage and the reduction of H2 O2 uptake thereby undermining the CPO activity. The mechanism appears generically applicable to other hemeproteins such as horseradish peroxidase, hemoglobin, and myoglobin. These findings may open new avenues for the design of peroxidase cascades for applications ranging from better diagnosis of diabetes to green synthesis of chemicals by direct functionalization of C−H bonds. Abstract : Peroxidase cascades : Glucose deactivates CPO through hydrophobic interaction with heme and hydrogen bonding with Glu 183 . These interactions lead to heme leakage and the reduction of H2 O2 uptake thereby undermining the CPO activity. The mechanism is applicable to horseradish peroxidase, hemoglobin, and myoglobin.