Copper–oxygen Dynamics in Tyrosinase

06 August 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


To unveil the activation of dioxygen on the copper centre (Cu2O2core) of tyrosinase, we performed X-ray crystallograpy with active-form tyrosinase at near atomic resolution. This study provided a novel insight into the catalytic mechanism of the tyrosinase, including the rearrangement of copper-oxygen species as well as the intramolecular migration of copper ion induced by substrate-binding.


oxygen activation
crystal structures
Catalytic mechanism
copper enzyme
dinuclear Cu enzymes
Michaelis Complex


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