Abstract
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 language | English (US) |
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Pages (from-to) | 382-386 |
Number of pages | 5 |
Journal | Inorganic Chemistry |
Volume | 35 |
Issue number | 2 |
DOIs | |
State | Published - 1996 |
Externally published | Yes |
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Inorganic Chemistry