Abstract
The introduction of a halogen atom into a small molecule can effectively modulate its properties, yielding bioactive substances of agrochemical and pharmaceutical interest. Consequently, the development of selective halogenation strategies is of high technological value. Besides chemical methodologies, enzymatic halogenations have received increased interest as they allow the selective installation of halogen atoms in molecular scaffolds of varying complexity under mild reaction conditions. Today, a comprehensive library of aromatic halogenases exists, and enzyme as well as reaction engineering approaches are being explored to broaden this enzyme family’s biocatalytic application range. In this review, we highlight recent developments in the sourcing, engineering, and application of flavin-dependent halogenases with a special focus on chemoenzymatic and coupled biosynthetic approaches.
Highlights
In nature, over 5000 halogenated products have been described since their first discovery over 100 years ago including potent antimicrobial agents such as vancomycin and chloramphenicol (Figure 1) [1]
Crystalvanadium, structures of flavin-dependent halogenases the presence of a chloride binding site near the flavin binding ependent halogenases follow an show electrophilic mechanism, while non-heme iron halogenase site [15,16], and mechanistic studies suggest that a nucleophilic attack of the chloride on the peroxyflavin alogenate through the formation of radical intermediates, and S-adenosyl-L-methionine
(3.0 h−1), this study described the production of chlorinated compounds by applying only light, halide salt, air, and FADH2 in aqueous solution [50]
Summary
Over 5000 halogenated products have been described since their first discovery over 100 years ago including potent antimicrobial agents such as vancomycin and chloramphenicol (Figure 1) [1]. Flavin-dependent halogenases (Fl-Hals) use reduced flavin, bound in the FAD binding site of the enzyme, to create a C4a-hydroperoxyflavin upon reaction with oxygen [11]. Crystalvanadium, structures of flavin-dependent halogenases the presence of a chloride binding site near the flavin binding ependent halogenases follow an show electrophilic mechanism, while non-heme iron halogenase site [15,16], and mechanistic studies suggest that a nucleophilic attack of the chloride on the peroxyflavin alogenate through the formation of radical intermediates, and S-adenosyl-L-methionine (SAM may create hypohalous acid (HOX) [11]. Flavin-dependent halogenases (Fl-Hals) use reduced flavin, bound in the FAD binding site o he enzyme, to create a C4a-hydroperoxyflavin species upon reaction with oxygen [11].
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