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Copper–Oxygen Dynamics in the Tyrosinase Mechanism
- Source :
- Angewandte Chemie International Edition. 59:13385-13390
- Publication Year :
- 2020
- Publisher :
- Wiley, 2020.
-
Abstract
- The dinuclear copper enzyme, tyrosinase, activates O2 to form a (μ-η2 :η2 -peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X-ray crystal structures of the active tyrosinases with substrate l-tyrosine. At their catalytic sites, CuA moved toward l-tyrosine (CuA1 → CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 → CuB2). The crystal structures and spectroscopic analyses of the dioxygen-bound tyrosinases demonstrated that the peroxide ligand rotated, spontaneously weakening its O-O bond. Thus, the copper migration induced by the substrate-binding is accompanied by rearrangement of the bound peroxide species so as to provide one of the peroxide oxygen atoms with access to the phenol substrate's ϵ carbon atom.
- Subjects :
- Aspergillus oryzae
Tyrosinase
chemistry.chemical_element
Crystal structure
Crystallography, X-Ray
010402 general chemistry
Photochemistry
01 natural sciences
Oxygen
Peroxide
Catalysis
Fungal Proteins
chemistry.chemical_compound
Bacterial Proteins
Catalytic Domain
Monophenol Monooxygenase
010405 organic chemistry
Ligand
Substrate (chemistry)
General Medicine
General Chemistry
Copper
Streptomyces
0104 chemical sciences
Models, Chemical
chemistry
Biocatalysis
Tyrosine
Protein Binding
Subjects
Details
- ISSN :
- 15213773 and 14337851
- Volume :
- 59
- Database :
- OpenAIRE
- Journal :
- Angewandte Chemie International Edition
- Accession number :
- edsair.doi.dedup.....30ac288234ccfa7f1751e07934cceb36