Lytic polysaccharide monooxygenases (LPMOs) have an essential role in global carbon
cycle, industrial biomass processing and microbial pathogenicity by catalysing the oxidative …

The discovery of oxidative cleavage of glycosidic bonds by enzymes currently known as lytic
polysaccharide monooxygenases (LPMOs) has profoundly changed our current …

Lytic polysaccharide monooxygenases (LPMOs) are powerful monocopper enzymes that
can activate strong C–H bonds through a mechanism that remains largely unknown. Herein …

One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

Lytic polysaccharide monooxygenases have received significant attention as catalytic
convertors of biomass to biofuel. Recent studies suggest that its peroxygenase activity (ie …

Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes that degrade the
insoluble crystalline polysaccharides cellulose and chitin. Besides the H 2 O 2 cosubstrate …

The enzymatic oxidation of methane to methanol was discovered in methanotrophs over 110
years ago. Nevertheless, the mechanism of action of particulate methane monooxygenase …

Electrons can tunnel through proteins in microseconds with a modest release of free energy
over distances in the 15 to 20 Å range. To span greater distances, or to move faster, multiple …

Oxidoreductases have evolved tyrosine/tryptophan pathways that channel highly oxidizing
holes away from the active site to avoid damage. Here we dissect such a pathway in a …

Lytic polysaccharide monooxygenases (LPMOs) have been proposed to react with both O 2
and H 2 O 2 as cosubstrates. In this study, the H 2 O 2 reaction with reduced Hypocrea …