ArticleInternational journal of molecular sciences2023
Quantum Mechanical Study of Oxygen Ligands Protonation for the Stable States of the Laccase Active Site.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Laccase Production Optimization from RecombinantMolecules (Basel, Switzerland) · 2024Article
- Structural Insight into the Amino Acid Environment of the Two-Domain Laccase's Trinuclear Copper Cluster.International journal of molecular sciences · 2023Article
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3 authors.
Funding
Abstract
Laccases are enzymes catalyzing the oxidation of a wide range of organic and inorganic substrates accompanied by molecular oxygen reduction to water. Recently, oxygen reduction by laccases has been studied by single-crystal serial X-ray crystallography with increasing absorption doses at subatomic resolution. There were two determined structures corresponding to the reduced and oxidized stable states of the laccase active site. However, the protonation of the oxygen ligands involved cannot be determined even at subatomic resolution. In the present work, the protonation of oxygen ligands in the active site of laccase for the two stable states determined in the X-ray study was explored using quantum mechanical and continuum-electrostatics calculations. This is important for understanding the reaction of the oxygen reduction mechanism in laccases. The high precision of X-ray data at subatomic resolutions allowed us to optimize the quantum mechanical calculations.
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