Engineering C–C Bond Cleavage Activity into a P450 Monooxygenase Enzyme

• Published in: Journal of the American Chemical Society Vol. 145; no. 16; pp. 9207 - 9222
• Main Authors: Miller, Justin C., Lee, Joel H. Z., Mclean, Mark A., Chao, Rebecca R., Stone, Isobella S. J., Pukala, Tara L., Bruning, John B., De Voss, James J., Schuler, Mary A., Sligar, Stephen G., Bell, Stephen G.
• Format: Journal Article
• Language: English
• Published: WASHINGTON American Chemical Society 26.04.2023; Amer Chemical Soc
• Subjects: active sites; benzoic acid; Catalysis; Catalytic Domain; chemical bonding; Chemistry; Chemistry, Multidisciplinary; cleavage (chemistry); cytochrome P-450; dealkylation; enzymes; epoxidation reactions; heme; Humans; hydroxylation; isotopes; Lyases; molecular dynamics; Molecular Dynamics Simulation; mutants; oxygen; Physical Sciences; Science & Technology; solvents; topology; COMPOUND I; CYP199A4; DEMETHYLASE; MECHANISM; CHOLESTEROL; CYTOCHROME P450CAM; SUBSTRATE; HYDROXYLATION; INHIBITORS; AROMATASE

The cytochrome P450 (CYP) superfamily of heme monooxygenases has demonstrated ability to facilitate hydroxylation, desaturation, sulfoxidation, epoxidation, heteroatom dealkylation, and carbon–carbon bond formation and cleavage (lyase) reactions. Seeking to study the carbon–carbon cleavage reaction...