Reduction Potentials of P450 Compounds I and II: Insight into the Thermodynamics of C-H Bond Activation.

ABSTRACT: We present a mixed experimental/theoretical determination of the bond strengths and redox potentials that define the ground-state thermodynamics for C-H bond activation in cytochrome P450 catalysis. Using redox titrations with [Ir(IV)Cl₆]^2-, we have determined the compound II/ferric (or Fe(IV)OH/Fe(III)OH₂) couple and its associated D(O-H)_Ferric bond strength in CYP158. Knowledge of this potential as well as the compound II/ferric (or Fe(IV)O/Fe(III)OH) reduction potential in horseradish peroxidase and the two-electron compound I/ferric (or Fe(IV)O(Por^•)/Fe(III)OH₂(Por)) reduction potential in aromatic peroxidase has allowed us to gauge the accuracy of theoretically determined bond strengths. Using the restricted open shell

SUBMITTER: Mittra K 

PROVIDER: S-EPMC7104868 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature