ArticleNature communications2024
Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Multifunctional lysozymes from the assassin bug Sycanus bifidus: Insecticidal proteins with anticoagulant and melanization inhibition properties.Pest management science · 2026Article
- Dose-dependent structural and electron-density features in the lytic polysaccharide monooxygenase NcAA9D.Acta crystallographica. Section D, Structural biology · 2026Article
- Empowering Precision C-H Functionalization: Advances in Peroxygenase Engineering.Angewandte Chemie (International ed. in English) · 2026Review
- Article
- 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
- Electron Transport through a Tryptophan Quadruplex in a Dimeric Azurin Construct.The journal of physical chemistry. B · 2026Article
- Electrochemical Insight into the Copper Redox Chemistry and HACS electrochemistry · 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
- Functional Characterization of Multidomain LPMOs from MarineBiochemistry · 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
- 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
- Electron transfer in polysaccharide monooxygenase catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Oxidoreductases have evolved tyrosine/tryptophan pathways that channel highly oxidizing holes away from the active site to avoid damage. Here we dissect such a pathway in a bacterial LPMO, member of a widespread family of C-H bond activating enzymes with outstanding industrial potential. We show that a strictly conserved tryptophan is critical for radical formation and hole transference and that holes traverse the protein to reach a tyrosine-histidine pair in the protein's surface. Real-time monitoring of radical formation reveals a clear correlation between the efficiency of hole transference and enzyme performance under oxidative stress. Residues involved in this pathway vary considerably between natural LPMOs, which could reflect adaptation to different ecological niches. Importantly, we show that enzyme activity is increased in a variant with slower radical transference, providing experimental evidence for a previously postulated trade-off between activity and redox robustness.
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Registered trials
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 Socratic graph.