Two decades ago, theoretical model calculations played a truly minor role in understanding
mechanisms of redox-active metalloenzymes. The methods available to treat transition …

Naturally produced halogenated compounds are ubiquitous across all domains of life where
they perform a multitude of biological functions and adopt a diversity of chemical structures …

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 …

Mononuclear non-heme Fe (II)-and 2-oxoglutarate (2OG)-dependent oxygenases comprise
a large family of enzymes that utilize an Fe (IV)-oxo intermediate to initiate diverse oxidative …

Selective functionalization of unactivated C–H bonds, water oxidation, and dioxygen
reduction are extremely important reactions in the context of finding energy carriers and …

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 …

The naphthyridinomycin biosynthesis enzyme NapI selectively performs the desaturation of
a free l-arginine amino acid at the C4–C5 bond as part of its antibiotic biosynthesis reaction …

The enzymatic generation of carbon–halogen bonds is a powerful strategy used by both
nature and synthetic chemists to tune the bioactivity, bioavailability and reactivity of …

Since our initial report in 1976, the oxygen rebound mechanism has become the consensus
mechanistic feature for an expanding variety of enzymatic C–H functionalization reactions …

Iron is an especially important redox-active cofactor in biology because of its ability to
mediate reactions with atmospheric O2. Iron-dependent oxygenases exploit this earth …