Preferential hydroxylation over epoxidation catalysis by a horseradish peroxidase mutant: A cytochrome P450 mimic

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Density functional theory calculations are presented on the catalytic properties of a horseradish peroxidase mutant whereby the axial nitrogen atom is replaced by phosphorus. This mutant has never been studied experimentally and only one theoretical report on this system is known (de Visser, S. P. J. Phys. Chem. B 2006, 110, 20759-20761). Thus, a one-atom substitution in horseradish peroxidase changes the properties of the catalytic center of the enzyme to more cytochrome P450-type qualities. In particular, the phosphorussubstituted horseradish peroxidase mutant reacts with substrates via a unique reactivity pattern, whereby alkanes are regioselectively hydroxylated even in the presence of a double bond. Reaction barriers of propene epoxidation and hydroxylation are almost identical to ones observed for a cytochrome P450 catalyst and significantly higher than those obtained for a horseradish peroxidase catalyst. It is shown that the regioselectivity difference is entropy and thermally driven and that the electron-transfer processes that occur during the reaction mechanism follow cytochrome P450-type patterns in the hydroxylation reaction. © 2007 American Chemical Society.
    Original languageEnglish
    Pages (from-to)12299-12302
    Number of pages3
    JournalJournal of Physical Chemistry B
    Volume111
    Issue number42
    DOIs
    Publication statusPublished - 25 Oct 2007

    Fingerprint

    Dive into the research topics of 'Preferential hydroxylation over epoxidation catalysis by a horseradish peroxidase mutant: A cytochrome P450 mimic'. Together they form a unique fingerprint.

    Cite this