Efficient regio- and stereo-selective C–H bond hydroxylation of steroids using an engineered heme-thiolate peroxygenase biocatalyst

Literature Information

Publication Date 2023-10-05
DOI 10.1039/D3CY01223A
Impact Factor 6.119
Authors

Jinia Akter, Eva F. Hayball, Stephen G. Bell


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Abstract

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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Catalysis Science & Technology

Catalysis Science & Technology
CiteScore: 5.91
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