Enhancing ferryl accumulation in H < sub > 2 < /sub > O < sub > 2 < /sub > -dependent cytochrome P450s

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.PMID:38141432 | DOI:10.1016/j.jinorgbio.2023.112458
Source: Journal of Inorganic Biochemistry - Category: Biochemistry Authors: Source Type: research