Copper is an essential trace element in living systems, present in the parts per million
concentration range. It is a key cofactor in a diverse array of biological oxidation-reduction …

Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

An unprecedentedly reactive iron species (2) has been generated by reaction of excess
peracetic acid with a mononuclear iron complex [FeII (CF3SO3) 2 (PyNMe3)](1) at cryogenic …

1.1. Background Copper proteins that bind and/or activate dioxygen perform a variety of
critical biological functions. 1-3 These include O2 transport (hemocyanin, Hc), 4 aromatic …

Spectroscopy has played a major role in developing our understanding of activesites in
copper proteins. Often these sites exhibit spectral features which are unique compared to …

Copper is an important element in oxidation catalysts for laboratory and industrial use.
Aerobic oxidation of 2, 6-xylenol with copper (I) in the presence of a N-donor ligand such as …

The considerable recent advances in copper–dioxygen coordination chemistry demonstrate
the existence of a variety of dioxygen-derived Cu nO 2 complexes, forming a basis for …

Dinuclear complexes containing metal centres in close proximity have been the subject of
recent extensive investigations since these structural units are thought to be involved in a …

The field of bioinorganic chemistry is still a rapidly growing area for research, which, despite
its title, encompasses many disciplines of chemistry and biology; synthetic organic chemists …

The kinetic and thermodynamic behavior of O2-binding to Cu (I) complexes can provide
fundamental understanding of copper (I)/dioxygen chemistry, which is of interest in chemical …