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Lin, Ying-Wu
Coordination chemistry reviews, 04/2017, Volume: 336Journal Article
Display omitted •Design of artificial metalloenzymes has achieved significant progress in the last decade.•Artificial metalloenzymes were designed from single to multiple active sites in native or de novo proteins.•Artificial metalloenzymes exhibit diverse functions, even beyond those of natural metalloenzymes.•The progress elucidates the structure-function relationship of natural metalloenzymes.•The progress provides clues for design of advanced artificial metalloenzymes with potential applications. Artificial metalloenzymes combine the advantages of both natural enzymes and chemically synthesized models, which have achieved significant progress in the last decade. This review summarizes the recent achievements in rational design of metalloenzymes from single to multiple active sites in natural or de novo protein scaffolds, with a diverse range of functionalities, even beyond those of natural metalloenzymes. These achievements include construction of mononuclear active site by metal substitution or incorporation, design of homo- or hetero-dinuclear site, introduction of Fe-sulfur or other metal clusters, reconstitution of metallo-porphyrins or other metal complexes, and design of dual or multiple active sites in single, dimeric proteins, de novo proteins, protein-protein interfaces, as well as protein oligomers and polymers. Other new trends in recent designs are also discussed. The progress not only elucidates the structural and functional relationship of natural metalloenzymes, but also provides practical clues for design of advanced artificial metalloenzymes with potential applications.
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