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 …

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 …

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

This reference on current VB theory and applications presents a practical system that can be
applied to a variety of chemical problems in a uniform manner. After explaining basic VB …

The Account discusses the phenomenon of two-state reactivity (TSR) or multistate reactivity
(MSR) in high-valent metal–oxo reagents, projecting its wide-ranging applicability starting …

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 …

Density functional theory is used to explore the mechanisms of alkane hydroxylation for four
synthetic non-heme iron (IV)− oxo complexes with three target substrates (Kaizer, J.; Klinker …

This review examines the monooxygenase, peroxidase and peroxygenase properties and
reaction mechanisms of cytochrome P450 (CYP) enzymes in bacterial, archaeal and …

Terpene cyclization, one of the most complex chemical reactions in nature, is generally
catalyzed by two classes of terpene cyclases (TCs). Cytochrome P450s that act as …

Using machine learning, molecular dynamics simulations, and density functional theory
calculations we gain insight into the selectivity patterns of substrate activation by the …