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

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

The cytochromes P450 constitute a large family of cysteinato-heme enzymes, 1-9 are
present in all forms of life (plants, bacteria, and mammals), and play a key role in the …

The title to a seminar presentation by IC Gunsalus in 1973 was “Oxygen: An essential toxin”,
referring to the complex role that atmospheric dioxygen has in biology. The relatively simple …

The introduction of oxygen into biochemical processes has brought about an evolutionary
leap in the history of life, whereby many organisms have evolved to use oxygen as part of …

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

Cytochrome P450 is one of the most versatile enzymes in nature. 1 It uses dioxygen and two
reducing equivalents to catalyze a great variety of stereospecific and regioselective oxygen …

Selective oxidation of saturated C–H bonds remains a challenge in modern chemistry. The
inert nature of such bonds requires the use of highly reactive reagents, and this poses major …

Enzymes are highly efficient catalysts in Nature that often react with high stereo-, chemo-,
and regioselectivity. Usually, enzymes achieve this selectivity through substrate binding and …

Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known.
The basic P450 reactions include C-hydroxylation, heteroatom oxygenation, heteroatom …