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Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl,...

Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl,...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_23770513

Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism

About this item

Full title

Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2014-01, Vol.111 (1), p.149-154

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

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 featu...

Alternative Titles

Full title

Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_jstor_primary_23770513

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_23770513

Other Identifiers

ISSN

0027-8424,1091-6490

E-ISSN

1091-6490

DOI

10.1073/pnas.1316609111

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