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Halogenases and dehalogenases: mechanisms; engineering; and applications
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DOI：10.1039/D5NP00055F.png)
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Abstract
En 中文
Halogenated organic compounds (HOCs) are essential building blocks in pharmaceuticals; agrochemicals; and advanced materials. However; their conventional chemical synthesis often relies on hazardous reagents and generates significant environmental waste. Harnessing nature's solutions; halogenases and dehalogenases offer selective; eco-friendly alternatives for the biosynthesis and degradation of HOCs. Halogenases; including electrophilic (e.g.; haloperoxidases; flavin-dependent); radical (α-ketoglutarate-dependent); and nucleophilic (S-adenosylmethionine (SAM)-dependent) types; facilitate precise C–X bond formation under mild conditions. Recent advances in protein engineering; such as the modification of tryptophan halogenases and fluorinases; have greatly expanded the repertoire and efficiency of biocatalytic halogenation; enabling the production of new-to-nature compounds for synthetic biology applications. In parallel; dehalogenases; ranging from reductive to hydrolytic and oxidative enzymes; play crucial roles in removing halogens from persistent pollutants; thereby supporting effective bioremediation and environmental detoxification. This review summarizes recent progress in enzyme discovery; mechanistic elucidation; protein engineering; and applied synthetic biology; with a focus on the integration of halogenases and dehalogenases into scalable platforms for both biosynthetic and remediation. Continued research aimed at improving enzyme stability; substrate scope; and operational robustness will be critical to fully realizing the industrial and environmental potential of these versatile biocatalysts.
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