The mechanism behind the oxidase activity of cellulose-active AA10 lytic polysaccharide monooxygenases

Using accurate quantum mechanics/molecular mechanics calculations, we show how an AA10 lytic polysaccharide monooxygenase generates hydrogen peroxide.

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Publication Details

Journal
Inorganic Chemistry Frontiers
Published
2025-01-01
DOI
https://doi.org/10.1039/d5qi00796h
Citations
3
Primary Topic
Enzyme-mediated dye degradation
Type
article
Field-Weighted Citation Impact
5.25
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article

The mechanism behind the oxidase activity of cellulose-active AA10 lytic polysaccharide monooxygenases

Ulf Ryde, Marlisa M. Hagemann, Erna K. Wieduwilt, Erik D. Hedegård
3 citations
Inorganic Chemistry Frontiers
Enzyme-mediated dye degradation
5.25
article

The mechanism behind the oxidase activity of cellulose-active AA10 lytic polysaccharide monooxygenases

Ulf Ryde, Marlisa M. Hagemann, Erna K. Wieduwilt, Erik D. Hedegård
article en
3 citations

Abstract

Using accurate quantum mechanics/molecular mechanics calculations, we show how an AA10 lytic polysaccharide monooxygenase generates hydrogen peroxide.

Inorganic Chemistry FrontiersVol. 12(18)
University of Southern Denmark (DK), Lund University (SE)
Openalex Percentile: Top 6%
Enzyme-mediated dye degradation
5.25
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