High-valent metal–oxo species with multiply-bonded M–O groups have been proposed as
key intermediates in many biological and abiological catalytic oxidation reactions. These …

Utilization of O2 as an abundant and environmentally benign oxidant is of great interest in
the design of bioinspired synthetic catalytic oxidation systems. Metalloenzymes activate O2 …

We report the reprogramming of nonheme iron enzymes to catalyze an abiological C (sp3)‒
H azidation reaction through iron-catalyzed radical relay. This biocatalytic transformation …

In nature, nonheme iron enzymes use dioxygen to generate high-spin iron (IV)= O species
for a variety of oxygenation reactions. Although synthetic chemists have long sought to …

The reduction of nitrogen (N2) to ammonia (NH3) is a requisite transformation for life.
Although it is widely appreciated that the iron-rich cofactors of nitrogenase enzymes facilitate …

Conspectus Mononuclear nonheme iron enzymes generate high-valent iron (IV)-oxo
intermediates that effect metabolically important oxidative transformations in the catalytic …

High-valent iron-oxo intermediates have often been implicated, and in some cases
identified, as the active oxidant in oxygen activating nonheme iron enzymes. Recent …

There have been significant advances in our understanding of mononuclear nonheme iron
oxygenases since our 1996 Chemical Reviews article, 1 promoted in large part by the many …

The most common catalyst in the Haber-Bosch process for the hydrogenation of dinitrogen
(N2) to ammonia (NH3) is an iron surface promoted with potassium cations (K+), but soluble …

High-valent iron (IV)–oxo species have been implicated as the key reactive intermediates in
the catalytic cycles of dioxygen activation by heme and non-heme iron enzymes. Our …