Synthesis, Structure, and Properties of a Model for Galactose Oxidase

Mei M. Whittaker, Walter R. Duncan, James W. Whittaker

Research output: Contribution to journalArticlepeer-review

92 Scopus citations


An active-site analog of the radical copper enzyme galactose oxidase has been prepared from a synthetic tripod chelate ((2-pyridylmethyl)[(2-hydroxy-3,5-dimethylphenyl)methyl][(2-hydroxy-5-methyl-3- (methylthio)phenyl)methyl]amine, duncamine (dnc)) that binds a single Cu(II) ion through phenolate, thioether-substituted phenolate, and pyridylamine arms. The Cu complex crystallizes as a dinucleated dimer bridged by phenolate oxygens, and the structure has been determined by X-ray crystallography. Addition of pyridine (or other coordinating bases) dissociates the complex into a monomeric derivative that has been characterized spectroscopically (optical absorption and EPR) and electrochemically. The model provides insight into the properties of a mutant form of galactose oxidase which retains the same copper ligand complement as the wild type protein but lacks catalytic activity.

Original languageEnglish (US)
Pages (from-to)382-386
Number of pages5
JournalInorganic Chemistry
Issue number2
StatePublished - Jan 1 1996

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

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