ArticleChemical science2025
Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.
Article in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- Experimental estimation of copper-site geometry reproducibility in biologically relevant redox and saccharide-bound states of a model lytic polysaccharide monooxygenase.Acta crystallographica. Section D, Structural biology · 2026Article
- Dose-dependent structural and electron-density features in the lytic polysaccharide monooxygenase NcAA9D.Acta crystallographica. Section D, Structural biology · 2026Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lytic polysaccharide monooxygenases (LPMOs) play a critical role in the depolymerization of recalcitrant polysaccharides, such as chitin, making them of interest in biotechnological applications. These interfacial enzymes are also of great chemical interest because of their unique monocopper catalytic center and their ability to activate high energy C-H bonds. This report investigates the structural and electronic changes at the copper (Cu) site of an LPMO,
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Registered trials
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