Ï- versus (Ï-1)-hydroxylation: Cytochrome P450 4B1 sterics make the call.

J Biol Chem. 2017 Mar 31;292(13):5622-5623

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Many family 4 cytochrome P450s play key roles in fatty acid hydroxylation at the terminal, or Ï, 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 Ï-hydroxylation is orchestrated by active-site sterics, partially mediated by an unusual heme-polypeptide ester bond.

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Ï- versus (Ï-1)-hydroxylation: Cytochrome P450 4B1 sterics make the call.

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Ï- versus (Ï-1)-hydroxylation: Cytochrome P450 4B1 sterics make the call.

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Ï- versus (Ï-1)-hydroxylation: Cytochrome P450 4B1 sterics make the call.