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A Catalytic Binding Site Together with a Distal Tyr in Myoglobin Affords Catalytic Efficiencies Similar to Natural Peroxidases

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成果类型:
期刊论文
作者:
Zhang, Ping;Yuan, Hong;Xu, Jiakun;Wang, Xiao-Juan;Gao, Shu-Qin;...
通讯作者:
Lin, Ying-Wu
作者机构:
[Lin, Ying-Wu; Wang, Xiao-Juan; Zhang, Ping] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
[Yuan, Hong; Tan, Xiangshi] Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China.
[Yuan, Hong; Tan, Xiangshi] Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China.
[Xu, Jiakun] Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fisheries, Qngdao 266071, Peoples R China.
[Gao, Shu-Qin; Lin, Ying-Wu] Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China.
通讯机构:
[Lin, Ying-Wu] U
Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China.
语种:
英文
关键词:
protein design;peroxidase;substrate binding site;X-ray crystallography;EPR;molecular docking
期刊:
ACS CATALYSIS
ISSN:
2155-5435
年:
2020
卷:
10
期:
1
页码:
891-896
基金类别:
It is a pleasure to acknowledge Prof. S. G. Sligar and Prof. Y. Lu of University of Illinois at Urbana–Champaign, for the kind gift of the sperm whale Mb gene. X-ray diffraction data were collected at Shanghai Synchrotron Radiation Facility (SSRF), China. EPR studies were performed on the Steady High Magnetic Field Facilities, High Magnetic Field Laboratory, Chinese Academy of Science. This work was supported by the National Natural Science Foundation of China (21977042), Special Scientific Research Funds for Central Nonprofit Institutes, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences (20603022016011), Financial Fund of the ministry of Agriculture and Rural Affairs, China (NFZX2018), and Human Provincial Innovation Foundation for Postgraduate (CX20190729).
机构署名:
本校为第一且通讯机构
院系归属:
化学化工学院
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...

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