ReviewCellular and molecular life sciences : CMLS2015
Electron transfer and reaction mechanism of laccases.
Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 146 papers.
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Who cites it
146 citing papers in PubMed, 581 citations in OpenAlex.
- Emerging classes of copper enzymes.Current opinion in chemical biology · 2026Review
- Decoding the distribution, structure-function-redox potential relationship and recent advances in fungal laccases: a systematic approach.Bioprocess and biosystems engineering · 2026Review
- Design, synthesis, and antifungal activity of anethole-based oxime ester compounds as potential laccase inhibitors.Pest management science · 2026Article
- Deciphering the Catalytic Mechanism of Oxidoreductase-Like Nanozymes Along the Reaction Pathway: Activity, Specificity and Sustainability.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Azurins With Tunable Reduction Potentials as Redox Mediators for Extracellular Electron Transfer.Chembiochem : a European journal of chemical biology · 2026Article
- Plant Biomass Depolymerization by Oxidoreductases: Structural Characteristics, Synergy Mechanism, and Evolutionary Adaptation.Journal of agricultural and food chemistry · 2026Review
- Hydrophobic tuning with non-canonical amino acids in a copper metalloenzyme.Nature chemistry · 2026Article
- Characterization and application potential of a robust recombinant laccase rTpLcc3 from Trametes polyzona for textile dye decolorization.Scientific reports · 2026Article
- Understanding Lignin Oxidation by a Two-Domain Multicopper Oxidase fromBiochemistry · 2026Article
- Genome-wide characterization of the LAC gene family in five fern species reveals evolutionary diversification and putative roles in lignin biosynthesis in Alsophila spinulosa.BMC plant biology · 2026Article
- Structural basis for organism-dependent effects on spectroscopic properties of type 1 copper azurin by the same axial methionine to histidine mutation.Journal of inorganic biochemistry · 2026Article
- Enhanced Inhibition ofInternational journal of molecular sciences · 2026Article
- Machine Learning Prediction of Laccase-Catalyzed Oxidation of Aromatic Compounds Using Curated Enzyme-Specific Datasets.Journal of computational chemistry · 2026Article
- A la carte bioprospecting of substrate-selective laccases via high-throughput computational enzyme-substrate interaction profiling.Protein science : a publication of the Protein Society · 2026Article
- Microbial and enzymatic biodegradation of aflatoxins and ochratoxins: mechanisms, applications, and emerging innovations.Archives of microbiology · 2026Review
- Condition-dependent expression of CotA laccase in Bacillus licheniformis reveals sporulation-linked activity and associated pigment formation.Archives of microbiology · 2026Article
- Advances in zearalenone-degrading enzymes research: characteristics, mining, improvement, and application.Journal of animal science and biotechnology · 2025Review
- Remolding laccase for whole-cell and in vivo modulation of dopamine signal.Science advances · 2025Article
- Engineering the Bacterial Laccase CotA for Functional Expression and Dye Decolorization Through Site-Directed Mutagenesis.Biology · 2025Article
- Multienzyme (3-in-1)-Mimicking a Single Nucleobase-Derived Bionanozyme for Versatile Environmental and Biomedical Applications.Advanced healthcare materials · 2025Article
86 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Laccases are part of the family of multicopper oxidases (MCOs), which couple the oxidation of substrates to the four electron reduction of O2 to H2O. MCOs contain a minimum of four Cu's divided into Type 1 (T1), Type 2 (T2), and binuclear Type 3 (T3) Cu sites that are distinguished based on unique spectroscopic features. Substrate oxidation occurs near the T1, and electrons are transferred approximately 13 Å through the protein via the Cys-His pathway to the T2/T3 trinuclear copper cluster (TNC), where dioxygen reduction occurs. This review outlines the electron transfer (ET) process in laccases, and the mechanism of O2 reduction as elucidated through spectroscopic, kinetic, and computational data. Marcus theory is used to describe the relevant factors which impact ET rates including the driving force, reorganization energy, and electronic coupling matrix element. Then, the mechanism of O2 reaction is detailed with particular focus on the intermediates formed during the two 2e(-) reduction steps. The first 2e(-) step forms the peroxide intermediate, followed by the second 2e(-) step to form the native intermediate, which has been shown to be the catalytically relevant fully oxidized form of the enzyme.
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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 OpenQuestion graph.