Engineering Cytochrome P450BM3 Enzymes for Direct Nitration of Unsaturated Hydrocarbons

Angew Chem Int Ed Engl. 2023 Mar 20;62(13):e202217678. doi: 10.1002/anie.202217678. Epub 2023 Feb 6.

Abstract

Applications of the peroxidase activity of cytochrome P450 enzymes in synthetic chemistry remain largely unexplored. We present herein a protein engineering strategy to increase cytochrome P450BM3 peroxidase activity for the direct nitration of aromatic compounds and terminal aryl-substituted olefins in the presence of a dual-functional small molecule (DFSM). Site-directed mutations of key active-site residues allowed the efficient regulation of steric effects to limit substrate access and, thus, a significant decrease in monooxygenation activity and increase in peroxidase activity. Nitration of several phenol and aniline compounds also yielded ortho- and para-nitration products with moderate-to-high total turnover numbers. Besides direct aromatic nitration by P450 variants using nitrite as a nitrating agent, we also demonstrated the use of the DFSM-facilitated P450 peroxidase system for the nitration of the vinyl group of styrene and its derivatives.

Keywords: Aromatic Compounds; Nitration; P450 Enzymes; Peroxidase; Terminal Aryl Olefins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cytochrome P-450 Enzyme System* / metabolism
  • Hydrocarbons*
  • Organic Chemicals
  • Peroxidases
  • Phenols / chemistry

Substances

  • Hydrocarbons
  • Cytochrome P-450 Enzyme System
  • Organic Chemicals
  • Phenols
  • Peroxidases