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Enhancing ferryl accumulation in H2O2-dependent cytochrome P450s.
Amaya, Jose A; Manley, Olivia M; Bian, Julia C; Rutland, Cooper D; Leschinsky, Nicholas; Ratigan, Steven C; Makris, Thomas M.
Affiliation
  • Amaya JA; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States of America.
  • Manley OM; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States of America; Department of Structural and Molecular Biochemistry, North Carolina State University, Raleigh, NC 27695, United States of America.
  • Bian JC; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States of America.
  • Rutland CD; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States of America.
  • Leschinsky N; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States of America.
  • Ratigan SC; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States of America.
  • Makris TM; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States of America; Department of Structural and Molecular Biochemistry, North Carolina State University, Raleigh, NC 27695, United States of America; Department of Chemistry, North Carolina State Unive
J Inorg Biochem ; 252: 112458, 2024 03.
Article de En | MEDLINE | ID: mdl-38141432
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.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Cytochrome P-450 enzyme system / Peroxyde d'hydrogène Langue: En Journal: J Inorg Biochem Année: 2024 Type de document: Article Pays d'affiliation: États-Unis d'Amérique
Texte intégral
Ajouter à My VHL
Imprimer
XML
PubMed Links
Recherche sur Google

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Cytochrome P-450 enzyme system / Peroxyde d'hydrogène Langue: En Journal: J Inorg Biochem Année: 2024 Type de document: Article Pays d'affiliation: États-Unis d'Amérique