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 …

Aerobic life on our planet relies on the use of molecular oxygen for energy as well as for
biosynthesis of important biological compounds in metabolic pathways. Thermodynamically …

The ability of copper proteins to process dioxygen at ambient conditions has inspired
numerous research groups to study their structural, spectroscopic and catalytic properties …

Ring-cleaving dioxygenases catalyze the oxygenolytic fission of catecholic compounds, a
critical step in the aerobic degradation of aromatic compounds by bacteria. Two classes of …

Mononuclear nonheme-Fe (II)-dependent oxygenases comprise an extended family of
oxidising enzymes, of which the 2-oxoglutarate-dependent oxygenases and related …

1. Introduction 7075 1.1. Di-oxygenase and mono-oxygenase enzymes 7075 1.2. Oxygen
activation by metal ions 7076 1.3. Reactivity of alkyl hydroperoxide intermediates 7077 2 …

This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

Non-heme iron enzymes catalyze a wide range of O2 reactions, paralleling those of heme
systems. Non-heme iron active sites are, however, much more difficult to study because they …

Ring-cleaving dioxygenases catalyze key reactions in the aerobic microbial degradation of
aromatic compounds. Many pathways converge to catecholic intermediates, which are …