Efficient regio- and stereo-selective C–H bond hydroxylation of steroids using an engineered heme-thiolate peroxygenase biocatalyst
Literature Information
Jinia Akter, Eva F. Hayball, Stephen G. Bell
A crucial reaction in chemical synthesis is the activation of unactivated carbon–hydrogen bonds in complex molecules. We demonstrate the regio- and stereo-selective hydroxlation of the steroids progesterone and androstenedione using the peroxygenase activity of an engineered bacterial cytochrome P450 enzyme, CYP154C8. By replacing a single amino acid of the I-helix we change this monooxygenase enzyme into a peroxygenase, enabling the efficient and selective biocatalytic formation of the 16α-hydroxy steroid metabolite.
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