As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply
of metalloproteins for oxidative metabolism and protection against reactive oxygen species …

Presented herein is a comprehensive account of the electronic structure of corrole
derivatives. Our knowledge in this area derives from a broad range of methods, including UV …

Enzymes are complex biological catalysts and are critical to life. Most oxidations of
chemicals are catalyzed by cytochrome P450 (P450, CYP) enzymes, which generally utilize …

An isolated Csingle bondH bond in a molecule has a very low reactivity owing to the large
kinetic barrier associated to the Csingle bondH bond cleavage and the apolar nature of this …

Many oxidation–reduction (redox) enzymes, particularly oxygenases, have roles in reactions
that make and break C–C bonds. The list includes cytochrome P450 and other heme-based …

Cytochromes P450 (P450 or CYP) are heme-containing enzymes that catalyze the
introduction of one atom of molecular oxygen into nonactivated C–H bonds, often in a regio …

Cytochrome P450 enzymes primarily catalyze mixed-function oxidation reactions, plus some
reductions and rearrangements of oxygenated species, eg prostaglandins. Most of these …

The cytochromes P450 (P450s or CYPs) constitute a large heme enzyme superfamily,
members of which catalyze the oxidative transformation of a wide range of organic …

This review briefly summarizes what was known about NOS enzymology at the time of the
Nobel Prize award in 1998 and then discusses from the author's perspective some of the …

Highlights•Selective oxyfunctionalizations are among the most challenging reactions in
organic synthesis.•Unspecific peroxygenases (UPO) are a diverse group of secreted fungal …