Site-selective enzymatic C-H amidation for synthesis of diverse lactams

In this study, we report engineered cytochrome P450 enzymes that perform unprecedented enantioselective C-H amidation reactions and control the site selectivity to divergently construct β-, -, and -lactams, completely overruling the inherent reactivities of the C-H bonds. The enzymes, expressed in Escherichia coli cells, accomplish this abiological carbon-nitrogen bond formation via reactive iron-bound carbonyl nitrenes generated from nature-inspired acyl-protected hydroxamate precursors. This transformation is exceptionally efficient (up to 1,020,000 total turnovers) and selective (up to 25:1 regioselectivity and 97%, please refer to compound 2v enantiomeric excess), and can be performed easily on preparative scale.
Source: ScienceNOW - Category: Science Authors: Tags: Biochemistry, Chemistry reports Source Type: news