Confronting PFAS persistence: enzymes catalyzing C-F bond cleavage.

Autor: Wackett LP; Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis, MN 55455, USA. Electronic address: wacke003@umn.edu.
Jazyk: angličtina
Zdroj: Trends in biochemical sciences [Trends Biochem Sci] 2024 Dec 05. Date of Electronic Publication: 2024 Dec 05.
DOI: 10.1016/j.tibs.2024.11.001
Abstrakt: Studies of enzymes catalyzing carbon-fluorine (C-F) bond cleavage have focused largely on a limited number of native microbial hydrolases that are reactive with the natural product fluoroacetate. Driven by widespread interest in biodegrading commercial fluorinated compounds, many of which are known as per- and polyfluorinated alkyl substances (PFAS), it is necessary to identify and engineer new enzymes. For example, some hydrolases react with -CF 2 - moieties, a common functionality in PFAS. Additional enzymatic C-F cleaving mechanisms catalyzed by reductases, lyases, and oxygenases have been identified via screening. Screening and evolving PFAS defluorination in bacteria is inhibited by the obligate release of toxic fluoride from C-F cleavage. Engineering greater fluoride tolerance in bacteria is a problem that must be solved in tandem with enzyme improvement.
Competing Interests: Declaration of interests No competing interests are declared.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: