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Updated: Sep 3, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
ω- versus (ω-1)-hydroxylation: Cytochrome P450 4B1 sterics make the call
1From the Departments of Medicinal Chemistry, Pharmacology, and Biophysics, University of Michigan, Ann Arbor, Michigan 48109 scottee@umich.edu.
Abstract:
Many family 4 cytochrome P450s play key roles in fatty acid hydroxylation at the terminal, or ω, carbon, but the mechanistic basis for this energetically disfavored regiostereochemistry has been less clear. A co-crystal structure of the rabbit family 4 enzyme CYP4B1 with its substrate octane reveals that the propensity for ω-hydroxylation is orchestrated by active-site sterics, partially mediated by an unusual heme-polypeptide ester bond.
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