The rational design of well-defined, first-row transition metal complexes that can activate
dioxygen has been a challenging goal for the synthetic inorganic chemist. The activation of …

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 …

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 …

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 …

Fe (II)/α-ketoglutarate (αKG)-dependent hydroxylases catalyze an amazing diversity of
reactions that result in protein side-chain modifications, repair of alkylated DNA/RNA …

In an era dominated by the utilization of hydrocarbon mixtures (ie, oil and natural gas) as
feedstocks for the chemical industry, the functionalization of CH bonds, particularly in a …

The slow oxygen reduction reaction (ORR) kinetics on Pt catalysts is among the most limiting
factors in the energy conversion efficiency of the state-of-the-art PEMFC. Also, Pt is scarcely …

Conspectus 2003 marked a banner year in the bioinorganic chemistry of mononuclear non-
heme iron enzymes. The first non-heme oxoiron (IV) intermediate (called J) was trapped and …

Iron-containing enzymes are one of Nature's main means of effecting key biological
transformations. The mononuclear non-heme iron oxygenases and oxidases have received …

The Fe (II)-and α-ketoglutarate (αKG)-dependent dioxygenases use mononuclear nonheme
iron centers to effect hydroxylation of their substrates and decarboxylation of their …