Glucose oxidase (GOX) catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone with the simultaneous reduction of enzyme-bound flavin.
GOX exists as a homodimer, with each subunit binding one FAD molecule.
Crystal structures show that FAD binds in a deep pocket of the enzyme near the dimer interface.
Studies showed that upon replacement of FAD with 8-hydroxy-5-carba-5-deaza FAD, the stereochemistry of the reaction was determined by reacting with the re face of the flavin.
During turnover, the neutral and anionic semiquinones are observed which indicates a radical mechanism.
Glucose oxidase (GOX) catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone with the simultaneous reduction of enzyme-bound flavin. GOX exists as a homodimer, with each subunit binding one FAD molecule. Crystal structures show that FAD binds in a deep pocket of the enzyme near the dimer interface. Studies showed that upon replacement of FAD with 8-hydroxy-5-carba-5-deaza FAD, the stereochemistry of the reaction was determined by reacting with the re face of the flavin. During turnover, the neutral and anionic semiquinones are observed which indicates a radical mechanism.
Flavin adenine dinucleotide