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. 2024 Mar:252:112458.
doi: 10.1016/j.jinorgbio.2023.112458. Epub 2023 Dec 20.

Enhancing ferryl accumulation in H2O2-dependent cytochrome P450s

Jose A Amaya  1 , Olivia M Manley  2 , Julia C Bian  1 , Cooper D Rutland  1 , Nicholas Leschinsky  1 , Steven C Ratigan  1 , Thomas M Makris  3
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Enhancing ferryl accumulation in H2O2-dependent cytochrome P450s

Jose A Amaya et al. J Inorg Biochem. 2024 Mar.

Abstract

A facile strategy is presented to enhance the accumulation of ferryl (iron(IV)-oxo) species in H2O2 dependent cytochrome P450s (CYPs) of the CYP152 family. We report the characterization of a highly chemoselective CYP decarboxylase from Staphylococcus aureus (OleTSA) that is soluble at high concentrations. Examination of OleTSA Compound I (CpdI) accumulation with a variety of fatty acid substrates reveals a dependence on resting spin-state equilibrium. Alteration of this equilibrium through targeted mutagenesis of the proximal pocket favors the high-spin form, and as a result, enhances Cpd-I accumulation to nearly stoichiometric yields.

Keywords: CYP152; Compound I; Cytochrome P450; Ferryl; Peroxygenase.

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Conflict of interest statement

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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