ArticleChemical science2020
The role of the active site tyrosine in the mechanism of lytic polysaccharide monooxygenase.
Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.Chemical science · 2025Article
- Synthesis and Characterization of Copper Complexes Featuring a Redox-Active ONO Ligand in Three Molecular Oxidation States.Inorganic chemistry · 2025Article
- Electron transfer in polysaccharide monooxygenase catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- 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
- Mapping the Initial Stages of a Protective Pathway that Enhances Catalytic Turnover by a Lytic Polysaccharide Monooxygenase.Journal of the American Chemical Society · 2023Article
- Histidine oxidation in lytic polysaccharide monooxygenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 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
- Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase.Chemical science · 2022Article
- Article
- Highly selective generation of singlet oxygen from dioxygen with atomically dispersed catalysts.Chemical science · 2022Article
- Oxidase enzymes as sustainable oxidation catalysts.Royal Society open science · 2022Review
- Estimating the accuracy of calculated electron paramagnetic resonance hyperfine couplings for a lytic polysaccharide monooxygenase.Computational and structural biotechnology journal · 2021Article
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Authors and funding
5 authors.
Funding
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Abstract
Catalytic breakdown of polysaccharides can be achieved more efficiently by means of the enzymes lytic polysaccharide monooxygenases (LPMOs). However, the LPMO mechanism has remained controversial, preventing full exploitation of their potential. One of the controversies has centered around an active site tyrosine, present in most LPMO classes. Recent investigations have for the first time obtained direct (spectroscopic) evidence for the possibility of chemical modification of this tyrosine. However, the spectroscopic features obtained in the different investigations are remarkably different, with absorption maximum at 420 and 490 nm, respectively. In this paper we use density functional theory (DFT) in a QM/MM formulation to reconcile these (apparently) conflicting results. By modeling the spectroscopy as well as the underlying reaction mechanism we can show how formation of two isomers (both involving deprotonation of tyrosine) explains the difference in the observed spectroscopic features. Both isomers have a [TyrO-Cu-OH]
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