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Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis
Frantisek Filandr1,2, Daniel Kavan1, Daniel Kracher3
1Institute of Microbiology of the CAS, Division BioCeV, Prumyslova 595, 252 50 Vestec, Czech Republic.
Biomolecules
|February 9, 2020
Summary
Lytic polysaccharide monooxygenases (LPMOs) undergo structural changes during catalysis. Substrate binding stabilizes LPMOs, but prolonged reduction causes oxidative damage, while cellulose protects against this damage.
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- Lytic polysaccharide monooxygenases (LPMOs) are crucial oxidoreductases for lignocellulose breakdown.
- Catalytic activity of LPMOs depends on the reduction of their active-site copper center.
Purpose of the Study:
- To investigate the structural basis of substrate-mediated stabilization in fungal LPMO9C from *Neurospora crassa*.
- To understand the effects of copper reduction and substrate interaction on LPMO structure and stability.
Main Methods:
- Advanced time-resolved mass spectrometry.
- Hydrogen/deuterium exchange mass spectrometry (HDX-MS).
Main Results:
- Copper reduction in *Nc*LPMO9C induces active-site structural rearrangements.
- Extended exposure to ascorbic acid leads to oxidative damage, unfolding, and fragmentation.
- Crystalline cellulose binding does not alter protein-wide hydrogen bonding or surface shielding.
- Cellulose protects LPMO from autooxidative damage caused by uncoupling reactions.
Conclusions:
- LPMO-substrate interactions are primarily mediated by side chains.
- Substrate binding confers a protective effect against catalytic damage.
- These findings provide insights into the dynamic structural changes governing LPMO catalysis.
Keywords:
hydrogen/deuterium exchange mass spectrometrylignocellulose degradationlytic polysaccharide monooxygenaseoxidative amino acid modificationpeptide bond cleavagereactive oxygen speciesMore Related Videos
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