Conversion of Human Neuroglobin into a Multifunctional Peroxidase by Rational Design

文献类型： 外文期刊

第一作者： Chen, Shun-Fa

作者： Chen, Shun-Fa;Liu, Xi-Chun;Lin, Ying-Wu;Xu, Jia-Kun;Lang, Jia-Jia;Wen, Ge-Bo;Lin, Ying-Wu;Li, Lianzhi

作者机构：

期刊名称：INORGANIC CHEMISTRY （ 影响因子：5.165； 五年影响因子：4.815 ）

ISSN： 0020-1669

年卷期： 2021 年 60 卷 4 期

页码：

收录情况： SCI

摘要： Protein design has received much attention in the last decades. With an additional disulfide bond to enhance the protein stability, human A15C neuroglobin (Ngb) is an ideal protein scaffold for heme enzyme design. In this study, we rationally converted A15C Ngb into a multifunctional peroxidase by replacing the heme axial His64 with an Asp residue, where Asp64 and the native Lys67 at the heme distal site were proposed to act as an acid-base catalytic couple for H2O2 activation. Kinetic studies showed that the catalytic efficiency of A15C/H64D Ngb was much higher (similar to 50-80-fold) than that of native dehaloperoxidase, which even exceeds (similar to 3-fold) that of the most efficient native horseradish peroxidase. Moreover, the dye-decolorizing peroxidase activity was also comparable to that of some native enzymes. Electron paramagnetic resonance, molecular docking, and isothermal titration calorimetry studies provided valuable information for the substrate-protein interactions. Therefore, this study presents the rational design of an efficient multifunctional peroxidase based on Ngb with potential applications such as in bioremediation for environmental sustainabllity.

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