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

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 …

Abstract Haematite (α-Fe2O3) has been extensively investigated as a photoanode in
photoelectrochemical water oxidation, but the product O2 has a low economic value. Here …

Iron is an especially important redox-active cofactor in biology because of its ability to
mediate reactions with atmospheric O2. Iron-dependent oxygenases exploit this earth …

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 …

TAML activators of peroxides are iron (III) complexes. The ligation by four deprotonated
amide nitrogens in macrocyclic motifs is the signature of TAMLs where the macrocyclic …

The metal–salen complexes (metal= Mn, Cr, Fe, Ru, Co, V and Ti) find widespread use as
efficient catalysts for the selective oxygenation of organic sulfides, sulfoxides and aromatic …

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

We have developed a metal‐free process for the aerobic photooxygenation of sulfides to
sulfoxides mediated by riboflavin tetraacetate or riboflavin (vitamin B2) photocatalysts and …

Redox-inactive metal ions play pivotal roles in regulating the reactivities of high-valent metal–
oxo species in a variety of enzymatic and chemical reactions. A mononuclear non-heme Mn …