Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis.

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ID: 93903
2020
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Abstract
Lytic polysaccharide monooxygenases (LPMOs) are industrially important oxidoreductases employed in lignocellulose saccharification. Using advanced time-resolved mass spectrometric techniques, we elucidated the structural determinants for substrate-mediated stabilization of the fungal LPMO9C from during catalysis. LPMOs require a reduction in the active-site copper for catalytic activity. We show that copper reduction in LPMO9C leads to structural rearrangements and compaction around the active site. However, longer exposure to the reducing agent ascorbic acid also initiated an uncoupling reaction of the bound oxygen species, leading to oxidative damage, partial unfolding, and even fragmentation of LPMO9C. Interestingly, no changes in the hydrogen/deuterium exchange rate were detected upon incubation of oxidized or reduced LPMO with crystalline cellulose, indicating that the LPMO-substrate interactions are mainly side-chain mediated and neither affect intraprotein hydrogen bonding nor induce significant shielding of the protein surface. On the other hand, we observed a protective effect of the substrate, which slowed down the autooxidative damage induced by the uncoupling reaction. These observations further complement the picture of structural changes during LPMO catalysis.
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filandr2020structuralbiomolecules Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Filandr, Frantisek;Kavan, Daniel;Kracher, Daniel;Laurent, Christophe V F P;Ludwig, Roland;Man, Petr;Halada, Petr;
Journal Biomolecules
Year 2020
DOI
E242
URL
Keywords
reactive oxygen species lignocellulose degradation hydrogen/deuterium exchange mass spectrometry lytic polysaccharide monooxygenase oxidative amino acid modification peptide bond cleavage

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