ArticlePLoS biology2018
Catalytic mechanism of the tyrosinase reaction toward the Tyr98 residue in the caddie protein.
Article in PLoS biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 63 citations in OpenAlex.
- Inhibition effects of Eucalyptus globules Labill. essential oil against tyrosinase.Scientific reports · 2025Article
- Coupled Binuclear Copper Sites in Biology: An Experimentally-Calibrated Computational Perspective.Coordination chemistry reviews · 2025Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2025Article
- High pressure-derived nonsymmetrical [CuScience advances · 2024Article
- Copper(II) Methacrylate Complexes with Imidazole Derivatives-Structural, Spectral and Antitumor Features.Molecules (Basel, Switzerland) · 2024Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Experimental Evidence and Mechanistic Description of the Phenolic H-Transfer to the CuJournal of the American Chemical Society · 2023Article
- Tyrosinase Inhibitors: A Perspective.Molecules (Basel, Switzerland) · 2023Review
- Enzymatic Electrochemical/Fluorescent Nanobiosensor for Detection of Small Chemicals.Biosensors · 2023Review
- New mechanistic insights into coupled binuclear copper monooxygenases from the recent elucidation of the ternary intermediate of tyrosinase.FEBS letters · 2023Review
- Article
- Elucidation of the tyrosinase/OProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Evidence for H-bonding interactions to the μ-ηChemical communications (Cambridge, England) · 2022Article
- Engineered tyrosinases with broadened bio-catalysis scope: immobilization using nanocarriers and applications.3 Biotech · 2021Review
- Recent advancements in enzyme-mediated crosslinkable hydrogels:APL bioengineering · 2021Review
- Considerations Regarding Activity Determinants of Fungal Polyphenol Oxidases Based on Mutational and Structural Studies.Applied and environmental microbiology · 2021Article
- Similar but Still Different: Which Amino Acid Residues Are Responsible for Varying Activities in Type-III Copper Enzymes?Chembiochem : a European journal of chemical biology · 2021Review
- AACS synthetic biology · 2021Article
- Histidine residues at the copper-binding site in human tyrosinase are essential for its catalytic activities.Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Identification of Amino Acid Residues Responsible for C-H Activation in Type-III Copper Enzymes by Generating Tyrosinase Activity in a Catechol Oxidase.Angewandte Chemie (International ed. in English) · 2020Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosinase (EC 1.14.18.1), a copper-containing monooxygenase, catalyzes the conversion of phenol to the corresponding ortho-quinone. The Streptomyces tyrosinase is generated as a complex with a "caddie" protein that facilitates the transport of two copper ions into the active center. In our previous study, the Tyr98 residue in the caddie protein, which is accommodated in the pocket of active center of tyrosinase, has been found to be converted to a reactive quinone through the formations of the μ-η2:η2-peroxo-dicopper(II) and Cu(II)-dopasemiquinone intermediates. Until now-despite extensive studies for the tyrosinase reaction based on the crystallographic analysis, low-molecular-weight models, and computer simulations-the catalytic mechanism has been unable to be made clear at an atomic level. To make the catalytic mechanism of tyrosinase clear, in the present study, the cryo-trapped crystal structures were determined at very high resolutions (1.16-1.70 Å). The structures suggest the existence of an important step for the tyrosinase reaction that has not yet been found: that is, the hydroxylation reaction is triggered by the movement of CuA, which induces the syn-to-anti rearrangement of the copper ligands after the formation of μ-η2:η2-peroxo-dicopper(II) core. By the rearrangement, the hydroxyl group of the substrate is placed in an equatorial position, allowing the electrophilic attack to the aromatic ring by the Cu2O2 oxidant.
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