ArticleBiomolecules2022
Protonation State of an Important Histidine from High Resolution Structures of Lytic Polysaccharide Monooxygenases.
Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Electrochemical Insight into the Copper Redox Chemistry and HACS electrochemistry · 2026Article
- Anions and citrate inhibit LsAA9A, a lytic polysaccharide monooxygenase (LPMO).The FEBS journal · 2025Article
- Article
- The rotamer of the second-sphere histidine in AA9 lytic polysaccharide monooxygenase is pH dependent.Biophysical journal · 2024Article
- Assessing the role of redox partners in TthLPMO9G and its mutants: focus on HBiotechnology for biofuels and bioproducts · 2024Article
- A Conserved Second Sphere Residue Tunes Copper Site Reactivity in Lytic Polysaccharide Monooxygenases.Journal of the American Chemical Society · 2023Article
- A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases.Nature communications · 2023Article
- 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
- Article
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Authors and funding
11 authors.
Funding
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Abstract
Lytic Polysaccharide Monooxygenases (LPMOs) oxidatively cleave recalcitrant polysaccharides. The mechanism involves (i) reduction of the Cu, (ii) polysaccharide binding, (iii) binding of different oxygen species, and (iv) glycosidic bond cleavage. However, the complete mechanism is poorly understood and may vary across different families and even within the same family. Here, we have investigated the protonation state of a secondary co-ordination sphere histidine, conserved across AA9 family LPMOs that has previously been proposed to be a potential proton donor. Partial unrestrained refinement of newly obtained higher resolution data for two AA9 LPMOs and re-refinement of four additional data sets deposited in the PDB were carried out, where the His was refined without restraints, followed by measurements of the His ring geometrical parameters. This allowed reliable assignment of the protonation state, as also validated by following the same procedure for the His brace, for which the protonation state is predictable. The study shows that this histidine is generally singly protonated at the Nε2 atom, which is close to the oxygen species binding site. Our results indicate robustness of the method. In view of this and other emerging evidence, a role as proton donor during catalysis is unlikely for this His.
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