Chemistry Letters · 1993 · 29 citations · 14 references
Life SciencesBiochemistryChemistryBiocatalysisEnzyme MechanismEnzymologyCoenzyme ChemistryCofactor ChemistryEnzyme BiophysicsOxidation ReactionsRedox CofactorsRedox EnzymesAbsorption SpectrumAbsorption Spectrum CalculationApoenzyme StructureElectron-withdrawing GroupsOxidation State AnalysisPhysicochemical PropertiesPulse RadiolysisRadical Species
Abstract Physicochemical properties of 2-methylthio-4-methylphenol (1) were examined in order to obtain information about the nature of the newly found cofactor of galactose oxidase. Electrochemical studies and theoretical calculations indicated that the methylthio group works as an electron-withdrawing substituent to stabilize the radical species (one-electron oxidation state) of 1. The absorption spectrum obtained by the pulse radiolysis of 1 was very close to that of the oxidized apoenzyme.
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Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase
Nobutoshi Ito, Simon E. V. Phillips, Conrad Stevens et al. · Nature · 1991 · 755 citations
The active site of galactose oxidase.
Mei M. Whittaker, James W. Whittaker · Journal of Biological Chemistry · 1988 · 212 citations · Full text