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Chemistry: Tyrosinase reactivity in a model complex: An alternative hydroxylation mechanism
Liviu M. Mirica
, Michael Vance
, Deanne Jackson Rudd
, Britt Hedman
, Keith O. Hodgson
, Edward I. Solomon
, T. Daniel P. Stack
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
DBBS - Biochemistry, Biophysics, and Structural Biology
Research output
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Contribution to journal
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Article
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peer-review
299
Scopus citations
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Keyphrases
Model Complex
100%
Tyrosinase
100%
Hydroxylation
100%
Phenolate
75%
Hydroxylated
25%
Catechol
25%
Absorption Spectra
25%
Bond Cleavage
25%
Reactive Intermediates
25%
Copper Enzymes
25%
Active Oxidants
25%
C-O Bond Formation
25%
Extreme Temperature
25%
Phenol Hydroxylation
25%
Binuclear Copper
25%
Nucleophilic Aromatic Substitution
25%
Bond Scission
25%
Substitution Mechanism
25%
Synthetic Enzyme Complex
25%
Chemistry
Chemistry
100%
Phenolate
100%
hydroxylation
100%
Catechol
33%
Reactive Intermediate
33%
Electrophilic Aromatic Substitution
33%
Phenol
33%
Absorption Spectra
33%
C-O bond formation
33%