ArticleEssays in biochemistry2023
Lytic polysaccharide monooxygenases: enzymes for controlled and site-specific Fenton-like chemistry.
Article in Essays in biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 59 citations in OpenAlex.
- Article
- High-Valent Late Transition Metal-Oxo Complexes: Breaking Boundaries at the Oxo Wall and Beyond.Chemical reviews · 2026Review
- Ligand Radicals Tune LPMO Activity in Model Complex.Inorganic chemistry · 2026Article
- Reduced Processivity in a Chitobiohydrolase Enhances LPMO-Assisted Chitin Depolymerization.Biochemistry · 2026Article
- Redox robustness drives LPMO evolution.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Investigation Into the Role of Reductants and Cosubstrates in Lytic Polysaccharide Monooxygenase Thermothielavioides terrestris AA9E Binding to Cellulose by Single-Molecule Imaging.Biotechnology and bioengineering · 2026Article
- Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.Chemical science · 2025Article
- Discovery of a Copper-Binding Carbohydrate-Binding Module Regulating the Activity of Lytic Polysaccharide Monooxygenases.Journal of the American Chemical Society · 2025Article
- Article
- Article
- Anions and citrate inhibit LsAA9A, a lytic polysaccharide monooxygenase (LPMO).The FEBS journal · 2025Article
- Structure-Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate Specificity.ACS catalysis · 2025Article
- Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions.FEBS letters · 2025Article
- Pinpointing Cu-Coordination Motifs in Bio-Inspired MOFs by Combining DFT-Assisted XAS Analysis and Multivariate Curve Resolution.The journal of physical chemistry. C, Nanomaterials and interfaces · 2025Article
- LPMO-Catalyzed Oxidation of Cellulosic Fibers with Controlled Addition of a Reductant and HACS sustainable chemistry & engineering · 2025Article
- Copper(II)-Oxyl Formation in a Biomimetic Complex Activated by Hydrogen Peroxide: The Key Role of Trans-Bis(Hydroxo) Species.Inorganic chemistry · 2024Article
- A Four-Coordinate End-On Superoxocopper(II) Complex: Probing the Link between Coordination Number and Reactivity.Journal of the American Chemical Society · 2024Article
- The impact of the carbohydrate-binding module on how a lytic polysaccharide monooxygenase modifies cellulose fibers.Biotechnology for biofuels and bioproducts · 2024Article
- Copper-oxygen adducts: new trends in characterization and properties towards C-H activation.Chemical science · 2024Review
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The discovery of oxidative cleavage of glycosidic bonds by enzymes currently known as lytic polysaccharide monooxygenases (LPMOs) has profoundly changed our current understanding of enzymatic processes underlying the conversion of polysaccharides in the biosphere. LPMOs are truly unique enzymes, harboring a single copper atom in a solvent-exposed active site, allowing them to oxidize C-H bonds at the C1 and/or C4 carbon of glycosidic linkages found in recalcitrant, often crystalline polysaccharides such as cellulose and chitin. To catalyze this challenging reaction, LPMOs harness and control a powerful oxidative reaction that involves Fenton-like chemistry. In this essay, we first draw a brief portrait of the LPMO field, notably explaining the shift from the monooxygenase paradigm (i.e., using O2 as cosubstrate) to that of a peroxygenase (i.e., using H2O2). Then, we briefly review current understanding of how LPMOs generate and control a hydroxyl radical (HO•) generated through Cu(I)-catalyzed H2O2 homolysis, and how this radical is used to create the proposed Cu(II)-oxyl species, abstracting hydrogen atom of the C-H bond. We also point at the complexity of analyzing redox reactions involving reactive oxygen species and address potential deficiencies in the interpretation of existing LPMO data. Being the first copper enzymes shown to enable site-specific Fenton-like chemistry, and maybe not the only ones, LPMOs may serve as a blueprint for future research on monocopper peroxygenases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.