A Catalytic Binding Site Together with a Distal Tyr in Myoglobin Affords Catalytic Efficiencies Similar to Natural Peroxidases
文献类型： 外文期刊
作者： Zhang, Ping 1 ; Yuan, Hong 2 ; Xu, Jiakun 4 ; Wang, Xiao-Juan 1 ; Gao, Shu-Qin 5 ; Tan, Xiangshi 2 ; Lin, Ying-Wu 1 ;
作者机构： 1.Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China
2.Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China
3.Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China
4.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fisheries, Qngdao 266071, Peoples R China
5.Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China
关键词： protein design; peroxidase; substrate binding site; X-ray crystallography; EPR; molecular docking
期刊名称：ACS CATALYSIS （ 影响因子：13.084； 五年影响因子：13.721 ）
ISSN： 2155-5435
年卷期： 2020 年 10 卷 1 期
页码：
收录情况： SCI
摘要： Functional enzyme design has made tremendous progress, but designer enzymes with activities comparable to those of natural enzymes are still limited. In this study, we rationally engineered a functional peroxidase with a catalytic binding site of guaiacol in a model protein, myoglobin (Mb), by replacing Phe46 with a serine (F46S mutation), together with a distal Tyr in the heme pocket (F43Y mutation). The double mutant F43Y/F46S Mb exhibited an overall catalytic efficiency that exceeds most natural peroxidases and is similar to the most efficient horseradish peroxidase. The catalytic substrate binding site was further confirmed by X-ray crystallography, EPR spectroscopy, and inhibition studies, as well as molecular docking simulations. Remarkably, this study reports an artificial peroxidase with an engineered catalytic binding site whose structure was solved both in the absence and presence of the substrate.
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