ArticleJournal of the American Chemical Society2023
Mapping the Initial Stages of a Protective Pathway that Enhances Catalytic Turnover by a Lytic Polysaccharide Monooxygenase.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Reversible hydrogen atom exchange between phenoxyl radical and phenol at cobalt(ii): role of coordination-induced bond activation.Chemical science · 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
- Ligand Radicals Tune LPMO Activity in Model Complex.Inorganic chemistry · 2026Article
- Redox robustness drives LPMO evolution.Proceedings of the National Academy of Sciences of the United States of America · 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
- 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
- Synthesis and Characterization of Copper Complexes Featuring a Redox-Active ONO Ligand in Three Molecular Oxidation States.Inorganic chemistry · 2025Article
- Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions.FEBS letters · 2025Article
- Article
- Mimicking the Reactivity of LPMOs with a Mononuclear Cu Complex.European journal of inorganic chemistry · 2024Article
- Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).Nature communications · 2024Article
- Understanding the initial events of the oxidative damage and protection mechanisms of the AA9 lytic polysaccharide monooxygenase family.Chemical science · 2024Article
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Authors and funding
21 authors at 5 institutions in 3 countries.
Funding
Abstract
Oxygenase and peroxygenase enzymes generate intermediates at their active sites which bring about the controlled functionalization of inert C-H bonds in substrates, such as in the enzymatic conversion of methane to methanol. To be viable catalysts, however, these enzymes must also prevent oxidative damage to essential active site residues, which can occur during both coupled and uncoupled turnover. Herein, we use a combination of stopped-flow spectroscopy, targeted mutagenesis, TD-DFT calculations, high-energy resolution fluorescence detection X-ray absorption spectroscopy, and electron paramagnetic resonance spectroscopy to study two transient intermediates that together form a protective pathway built into the active sites of copper-dependent lytic polysaccharide monooxygenases (LPMOs). First, a transient high-valent species is generated at the copper histidine brace active site following treatment of the LPMO with either hydrogen peroxide or peroxyacids in the absence of substrate. This intermediate, which we propose to be a Cu
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