A growing subset of metalloenzymes activates dioxygen with nonheme diiron active sites to
effect substrate oxidations that range from the hydroxylation of methane and the …

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

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 …

In recent years, significant progress has been made in understanding the geometric and
electronic structures of the active sites of non-heme iron enzymes and the contributions of …

Protein Radicals in Enzyme Catalysis. [Chem. Rev. 1998, 98, 705−762 | Chemical Reviews ACS
ACS Publications C&EN CAS Find my institution Log In Chemical Reviews ACS Publications …

Dioxygen activation by metalloenzymes generally proceeds through one of two
fundamentally different routes. Some enzymes, such as the ferric ion containing intradiol …

The Fe (II)-and α-ketoglutarate (αKG)-dependent dioxygenases have roles in synthesis of
collagen and sensing of oxygen in mammals, in acquisition of nutrients and synthesis of …

Oxidase and oxygenase enzymes allow the use of relatively unreactive O2 in biochemical
reactions. Many of the mechanistic strategies used in nature for this key reaction are …

Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to
deoxynucleotides in all organisms (eq 1). 1-3 These enzymes play an essential role in DNA …

Methanotrophic bacteria are capable of using methane as their sole source of carbon and
energy. The first step in methane metabolism, the oxidation of methane to methanol, is …