ArticleACS catalysis2026
Bacterial cytochrome P450 for oxidative halogenated biaryl coupling.
Article in ACS catalysis, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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9 authors.
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Abstract
Biaryl motifs are fundamental structural elements in many pharmaceuticals, agrochemicals, and advanced materials. Traditional synthetic approaches for biaryl bond formation often require harsh conditions, costly catalysts, and pre-functionalized starting materials, which limit their efficiency, sustainability, and substrate scope. Enzymatic catalysis offers a greener alternative. However, biocatalysts capable of directly coupling halogenated biaryl compounds remain largely underexplored. Here, we report the functional characterization of the marine-derived cytochrome P450 enzyme Bmp7, which catalyzes the formation of halogenated biaryls. We first characterized the product profile of recombinant Bmp7 using its native substrate 2,4-dibromophenol (
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