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Copper–oxygen Dynamics in Tyrosinase

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

Abstract

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.

Keywords

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

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Version History

Aug 06, 2019 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv.9255251.v1
D O I: 10.26434/chemrxiv.9255251.v1 [opens in a new tab]

Funding

JSPS KAKENHI Grant Number JP15K13743
JSPS KAKENHI Grant Number JP15H01066
JSPS KAKENHI Grant Number JP17H05233
JSPS KAKENHI Grant Number JP16H01025
JSPS KAKENHI Grant Number JP18H04270
JST CREST (# JPMJCR16P1)
Kao Melanin Workshop

Author’s competing interest statement

No conflict of interest.

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