Conversion of Human Neuroglobin into a Multifunctional Peroxidase by Rational Design
| Autor: | Xi-Chun Liu, Ying-Wu Lin, Ge-Bo Wen, Shun-Fa Chen, Jia-Kun Xu, Jia-Jia Lang, Lianzhi Li |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Protein Conformation
Protein design Neuroglobin Crystallography X-Ray 010402 general chemistry 01 natural sciences Horseradish peroxidase Inorganic Chemistry chemistry.chemical_compound Humans Physical and Theoretical Chemistry Heme Peroxidase chemistry.chemical_classification biology 010405 organic chemistry Electron Spin Resonance Spectroscopy Rational design Isothermal titration calorimetry Combinatorial chemistry 0104 chemical sciences Molecular Docking Simulation Enzyme chemistry biology.protein |
| Zdroj: | Inorganic Chemistry. 60:2839-2845 |
| ISSN: | 1520-510X 0020-1669 |
| Popis: | 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 (∼50-80-fold) than that of native dehaloperoxidase, which even exceeds (∼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 sustainability. |
| Databáze: | OpenAIRE |
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