Over time, organisms have evolved strategies to cope with the abundance of dioxygen on
Earth. Oxygen-utilizing enzymes tightly control the reactions involving O2 mostly by …

The reaction of flavoenzymes with oxygen remains a fascinating area of research because
of its relevance for reactive oxygen species (ROS) generation. Several exciting recent …

The ubiquitous flavin-dependent monooxygenases commonly catalyze oxygenation
reactions by means of a transient C4a–peroxyflavin. A recent study, however, suggested an …

Many flavoenzymes oxidases and monooxygenases react faster with oxygen than free
flavins do. There are many ideas on how enzymes cause this. Recent work has focused on …

This review article describes the occurrence, general properties, and substrate specificity of
the flavoenzymes belonging to the glucose-methanol-choline oxidoreductase superfamily …

The crystal structure of aryl-alcohol oxidase (AAO), a flavoenzyme involved in lignin
degradation, reveals two active-site histidines, whose role in the two enzyme half-reactions …

C4a-hydroperoxyflavin is found commonly in the reactions of flavin-dependent
monooxygenases, in which it plays a key role as an intermediate that incorporates an …

Herein, we report an enzymatic cascade involving an oxidase, an imine reductase and a
hydrogenase for the H2-driven synthesis of N-heterocycles. Variants of putrescine oxidase …

In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes
at the global scale. To clarify both the nature of the mechanism and possible differences in …

The ability of flavoenzymes to reduce dioxygen varies greatly, and is controlled by the
protein environment, which may cause either a rapid reaction (oxidases) or a sluggish …