In chemical terms, the regio-and stereoselective hydroxylation of hydrocarbon CH bonds is a
very difficult transformation. Nevertheless, these reactions are deftly catalyzed by a variety of …

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 …

Cytochromes P450 constitute a broad class of heme monooxygenase enzymes with more
than 11,500 isozymes which have been identified in organisms from all biological kingdoms …

OleT is a cytochrome P450 that catalyzes the hydrogen peroxide-dependent metabolism of
C n chain-length fatty acids to synthesize C n-1 1-alkenes. The decarboxylation reaction …

The cytochrome P450 monooxygenases (P450s) are thiolate heme proteins that can, often
under physiological conditions, catalyze many distinct oxidative transformations on a wide …

In contrast to the wide spectrum of cytochrome P450 monooxygenases, there are only 2
heme-based dioxygenases in humans: tryptophan dioxygenase (hTDO) and indoleamine 2 …

Establishing redox and thermodynamic relationships between metal-ion-bound O2 and its
reduced (and protonated) derivatives is critically important for a full understanding of (bio) …

Nanodiscs have proven to be a versatile tool for the study all types of membrane proteins,
including receptors, transporters, enzymes and viral antigens. The self-assembled Nanodisc …

Unlike photosystem II (PSII) that catalyzes formation of the O–O bond, the cytochromes P450
(P450), members of a superfamily of hemoproteins, catalyze the scission of the O–O bond of …