title: Stabilization of an intermediate in the oxidative half-reaction of human liver glycolate oxidase.
abstract: Glycolate oxidase is a flavin-dependent enzyme that catalyzes the oxidation of α-hydroxy acids to the corresponding α-keto acids, with reduction of molecular oxygen to hydrogen peroxide. A number of probes have been used to investigate the oxidative half-reaction catalyzed by the enzyme, including steady state and rapid kinetics, pH studies, solvent kinetic isotope effects, and solvent viscosity effects. Here we present the first spectroscopic evidence of the formation of an intermediate with absorbance features resembling those of a flavosemiquinone in the oxidative half-reaction of glycolate oxidase.
authors.affiliation: Department of Chemistry, Georgia State University, Atlanta, Georgia 30302-4098, United States.
authors.forename: Andrea
authors.initials: A
authors.lastname: Pennati
authors.forename: Giovanni
authors.initials: G
authors.lastname: Gadda
mesh_terms: D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D005415:Flavins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D013053:Spectrophotometry
chemical_list: D005415:Flavins; D000429:Alcohol Oxidoreductases; C020821:glycollate oxidase