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- W2892068522 abstract "The design of functional metalloenzymes is attractive, but few designs can exceed the catalytic rate of native enzymes. In order to create an effective artificial dehaloperoxidase (DHP), we redesigned the heme center of myoglobin (Mb) by introducing a distal Tyr43 and replacing the distal His64 with an Asp, which combines the structural features of chloroperoxidase (a distal Asp) with DHP (a distal Tyr). The rationally designed F43Y/H64D Mb was shown to exhibit a remarkable dehalogenation activity, with a catalytic efficiency more than 1000-fold higher than that of a native DHP from A. ornata. To the best of our knowledge, this is the highest activity reported to date for an artificial DHP. Moreover, X-ray structures of F43Y/H64D Mb and in complex with a typical substrate, 2,4,6-trichlorophenol (TCP), revealed a distal substrate binding site and crucial roles of both distal Tyr43 and Asp64. This study not only provides insights into the structure and function relationship of native and artificial DHPs but also suggests potential applications in bioremediation of toxic halophenols." @default.
- W2892068522 created "2018-09-27" @default.
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- W2892068522 date "2018-09-17" @default.
- W2892068522 modified "2023-10-16" @default.
- W2892068522 title "A Rationally Designed Myoglobin Exhibits a Catalytic Dehalogenation Efficiency More than 1000-Fold That of a Native Dehaloperoxidase" @default.
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- W2892068522 doi "https://doi.org/10.1021/acscatal.8b02979" @default.
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