Jonathan Rittle

TL;DR: The spectroscopic and kinetic characterization of the long-sought principal intermediate involved in this process, P450 compound I (P450-I), which was prepared in approximately 75% yield by reacting ferric CYP119 with m-chloroperbenzoic acid is reported.

TL;DR: Results indicate that a single iron site may be capable of stabilizing the various NxHy intermediates generated during catalytic NH3 formation, and propose that the interstitial carbon atom recently assigned in the nitrogenase cofactor may have a similar role, perhaps by enabling a singleIron site to mediate the enzymatic catalysis through a flexible iron–carbon interaction.

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 synthesis and isolation of a diamagnetic, 5-coordinate Fe═NNH2(+) species supported by a tris(phosphino)silyl ligand via the direct protonation of a terminally bound Fe-N2(-) complex is reported, demonstrating that an iron site can shuttle from a distal intermediate to an alternating intermediate en route to NH3 liberation from N2.

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.