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 …

Flavoprotein monooxygenases (FPMOs) are single-or two-component enzymes that
catalyze a diverse set of chemo-, regio-and enantioselective oxyfunctionalization reactions …

Covering: up to July 2019 Terpene synthases (TSs) are responsible for generating much of
the structural diversity found in the superfamily of terpenoid natural products. These elegant …

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 …

Oxygenases, which catalyze the reductive activation of O2 and incorporation of oxygen
atoms into substrates, are widely distributed in aerobes. They function by switching the …

LadA, a long-chain alkane monooxygenase, utilizes a terminal oxidation pathway for the
conversion of long-chain alkanes (up to at least C36) to corresponding primary alcohols in …

The ubiquitous flavoenzymes commonly catalyze redox chemistry such as the
monooxygenation of organic substrates and are both widely utilized in nature (eg, in primary …

Flavin-dependent monooxygenases (FDMOs) are known for their remarkable versatility and
for their crucial roles in various biological processes and applications. Extensive research …

Dioxygen (O2) and other gas molecules have a fundamental role in a variety of enzymatic
reactions. However, it is only poorly understood which O2 uptake mechanism enzymes …

One of the hallmark reactions catalyzed by flavin-dependent enzymes is the incorporation of
an oxygen atom derived from dioxygen into organic substrates. For many decades, these …