ArticleBiochemistry2023
Following the Fate of Lytic Polysaccharide Monooxygenases under Oxidative Conditions by NMR Spectroscopy.
Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- 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
- Harnessing the potential of lignocellulosic biomass for biofuels production.Applied microbiology and biotechnology · 2026Review
- Protein engineering and high-throughput screening of lytic polysaccharide monooxygenases: strategies, challenges, and prospects for industrial applications.World journal of microbiology & biotechnology · 2026Review
- Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.Chemical science · 2025Article
- A Molecular Mechanism for the Reduction of the Cu Site in Lytic Polysaccharide Monooxygenases by Phenol Reductants.JACS Au · 2025Article
- A suicidal and extensively disordered luciferase with a bright luminescence.Protein science : a publication of the Protein Society · 2024Article
- Assessing the role of redox partners in TthLPMO9G and its mutants: focus on HBiotechnology for biofuels and bioproducts · 2024Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of polysaccharides, such as cellulose and chitin. LPMO catalysis requires a reductant, such as ascorbic acid, and hydrogen peroxide, which can be generated in situ in the presence of molecular oxygen and various electron donors. While it is known that reduced LPMOs are prone to autocatalytic oxidative damage due to off-pathway reactions with the oxygen co-substrate, little is known about the structural consequences of such damage. Here, we present atomic-level insights into how the structure of the chitin-active
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