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The Third Generation of Artificial Dye-Decolorizing Peroxidase Rationally Designed in Myoglobin

文献类型： 外文期刊

作者： Zhang, Ping 1 ; Xu, Jiakun 2 ; Wang, Xiao-Juan 1 ; He, Bo 1 ; Gao, Shu-Qin 4 ; Lin, Ying-Wu 1 ;

作者机构： 1.Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China

2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fisheries, Qingdao 266071, Shandong, Peoples R China

3.Lab Marine Drugs & Byprod Pilot Natl Lab Marine S, Qingdao 266071, Shandong, Peoples R China

4.Univ South China, Tab Prot Struct & Funct, Hengyang 421001, Peoples R China

关键词： dye-decolorizing peroxidases; artificial enzyme; protein design; myoglobin; substrate-binding; 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： 2019 年 9 卷 9 期

页码：

收录情况： SCI

摘要： Approaches to degradation of industrial dyes are desirable, of which bioremediation is more favorable. In addition to the use of native enzymes, rational design of artificial enzymes provides an alternative approach. Meanwhile, few designs can achieve a catalytic activity comparable to that of native enzymes. We have previously designed two generations of artificial dye-decolorizing peroxidases (DyPs) in myoglobin (Mb) by introduction of Tyr43 and Trp138 in the heme pocket; however, the activity is moderate. To improve the activity of the artificial DyP, we herein designed a third generation by introduction of an additional Trp (P88W) to the protein surface, named F43Y/F138W/P88W Mb. The third generation of artificial DyP was shown to exhibit a catalytic efficiency exceeding that of various native DyPs and comparable to that of the most efficient native DyPs. Titration of reactive blue 19 (RB19) and molecular docking studies revealed crucial roles of Trp88 in substrate binding and oxidation, which acts as a catalytic site. This study not only provides clues for heme protein design but also suggests that the artificial DyP has potential applications for bioremediation in the future.

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