Timothy H. Yosca

TL;DR: The preparation of an iron(IV)hydroxide complex in a P450 enzyme (CYP158) in ≥90% yield is reported on, indicating that this elevated pKa results in a >10,000-fold reduction in the rate constant for oxidations of the protein framework, making these processes noncompetitive with substrate oxidation.

TL;DR: The importance of enzyme purification in the quest for reactive intermediates is examined and the preparation of compound I in a second P450 (P450ST) is reported and the validity of controversial reports claiming the production of P450 compound I through the use of peroxynitrite and laser flash photolysis is examined.

TL;DR: Weaker hydrogen bonding in P450-I results in a shorter Fe-S bond, which enables greater electron donation from the axial-thiolate ligand, which may in part explain P450's greater propensity for C-H bond activation.

TL;DR: The reaction of this species with a series of substituted radicals allows for the direct interrogation of the rebound process, providing insight into this uniformly invoked, but previously unobserved process.

TL;DR: New, fundamental insights are provided regarding the influence of axial donors on high-valent MnV(O) porphyrinoid complexes based upon a change in mechanism that hinges on the ability of the [MnV( O)(TBP8Cz)(X)]− complexes to function as either an electrophilic or weak nucleophilic oxidant depending upon the nature of the para-X substituents.