- Abstract:
-
Lytic polysaccharide monooxygenases (LPMOs) exhibit a mononuclear copper-containing active site and use dioxygen and a reducing agent to oxidatively cleave glycosidic linkages in polysaccharides. LPMOs represent a unique paradigm in carbohydrate turnover and exhibit synergy with hydrolytic enzymes in biomass depolymerization. To date, several features of copper binding to LPMOs have been elucidated, but the identity of the reactive oxygen species and the key steps in the oxidative mechanism h...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1073/pnas.1316609111
-
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- Journal:
- Proceedings of the National Academy of Sciences of the United States of America
- Volume:
- 111
- Issue:
- 1
- Pages:
- 149-154
- Publication date:
- 2014-01-05
- DOI:
- EISSN:
-
1091-6490
- ISSN:
-
0027-8424
- URN:
-
uuid:16065387-d09a-44d7-a884-7ada4593d923
- Source identifiers:
-
444271
- Local pid:
- pubs:444271
- Copyright date:
- 2014
Journal article
Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism.
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