ArticleThe Journal of biological chemistry2014
Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 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
- Protein engineering and high-throughput screening of lytic polysaccharide monooxygenases: strategies, challenges, and prospects for industrial applications.World journal of microbiology & biotechnology · 2026Review
- Impact of N-terminal acetylation on Cu(I) coordination by alpha synuclein protein.Journal of inorganic biochemistry · 2026Article
- Coupled on-line in crystallo UV-Vis absorption spectroscopy and X-ray crystallography to compare specific radiation damage in metal-containing proteins at room versus cryogenic temperature.Acta crystallographica. Section D, Structural biology · 2026Article
- Electrochemical Insight into the Copper Redox Chemistry and HACS electrochemistry · 2026Article
- Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.Chemical science · 2025Article
- Histidine-Copper Site Variability in UiO-66: Monitoring Synthetic Intricacy with EPR Spectroscopy.Chemistry of materials : a publication of the American Chemical Society · 2025Article
- Functional characterization of Lytic Polysaccharide Monooxygenase from Enterococcus mundtii CRi_37 for enhanced stubble saccharification.Molecular biology reports · 2025Article
- Enabling a bioinspiredDalton transactions (Cambridge, England : 2003) · 2024Article
- The rotamer of the second-sphere histidine in AA9 lytic polysaccharide monooxygenase is pH dependent.Biophysical journal · 2024Article
- A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A Conserved Second Sphere Residue Tunes Copper Site Reactivity in Lytic Polysaccharide Monooxygenases.Journal of the American Chemical Society · 2023Article
- Emerging Time-Resolved X-Ray Diffraction Approaches for Protein Dynamics.Annual review of biophysics · 2023Review
- Revisiting the role of electron donors in lytic polysaccharide monooxygenase biochemistry.Essays in biochemistry · 2023Review
- Structural and functional characterization of the catalytic domain of a cell-wall anchored bacterial lytic polysaccharide monooxygenase from Streptomyces coelicolor.Scientific reports · 2023Article
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Molecular Mechanism of Substrate Oxidation in Lytic Polysaccharide Monooxygenases: Insight from Theoretical Investigations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Review
- Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase.Chemical science · 2022Article
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12 authors.
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Abstract
Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes that employ a copper-mediated, oxidative mechanism to cleave glycosidic bonds. The LPMO catalytic mechanism likely requires that molecular oxygen first binds to Cu(I), but the oxidation state in many reported LPMO structures is ambiguous, and the changes in the LPMO active site required to accommodate both oxidation states of copper have not been fully elucidated. Here, a diffraction data collection strategy minimizing the deposited x-ray dose was used to solve the crystal structure of a chitin-specific LPMO from Enterococcus faecalis (EfaCBM33A) in the Cu(II)-bound form. Subsequently, the crystalline protein was photoreduced in the x-ray beam, which revealed structural changes associated with the conversion from the initial Cu(II)-oxidized form with two coordinated water molecules, which adopts a trigonal bipyramidal geometry, to a reduced Cu(I) form in a T-shaped geometry with no coordinated water molecules. A comprehensive survey of Cu(II) and Cu(I) structures in the Cambridge Structural Database unambiguously shows that the geometries observed in the least and most reduced structures reflect binding of Cu(II) and Cu(I), respectively. Quantum mechanical calculations of the oxidized and reduced active sites reveal little change in the electronic structure of the active site measured by the active site partial charges. Together with a previous theoretical investigation of a fungal LPMO, this suggests significant functional plasticity in LPMO active sites. Overall, this study provides molecular snapshots along the reduction process to activate the LPMO catalytic machinery and provides a general method for solving LPMO structures in both copper oxidation states.
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