期刊
NATURE CHEMICAL BIOLOGY
卷 12, 期 4, 页码 298-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.2029
关键词
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资金
- UK Biotechnology and Biological Sciences Research Council [BB/L000423, BB/L021633/1]
- Agence Francaise de l'Environnement et de la Maitrise de l'Energie [1201C102]
- Danish Council for Strategic Research [12-134923, 12-134922]
- European Community [283570]
- Institut de Chimie Moleculaire de Grenoble [FR 2607]
- LabEx ARCANE [ANR-11-LABX-0003-01]
- PolyNat Carnot Institute
- French Agence Nationale de la Recherche [PNRB2005-11]
- Biotechnology and Biological Sciences Research Council [BB/L021633/1, BB/L000423/1] Funding Source: researchfish
- BBSRC [BB/L021633/1, BB/L000423/1] Funding Source: UKRI
Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains.
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