PMID: 9436625Jan 22, 1998Paper

Single electron reduction of xenobiotic compounds by glucose oxidase from Aspergillus niger

Free Radical Biology & Medicine
C A Metosh-DickeyG W Winston

Abstract

Various species of fungi express glucose oxidase that catalyzes formation of gluconolactone from glucose with concomitant, direct divalent reduction of molecular oxygen to hydrogen peroxide. A physiological function ascribed to this extracellular enzyme is production of hydrogen peroxide for use in lignin degradation catalyzed by lignin peroxidases. Herein, we show that glucose oxidase can catalyze one-electron reduction of several different classes of xenobiotic compounds resulting in generation of free radical products. Electron spin resonance (ESR) spectroscopy was used to visualize the one-electron reduction products of 4-nitropyridine-N-oxide (4NPO), 1,4-naphthoquinone (1,4NQ), and dichlorophenolindolphenol (DCPIP). Hyperfine splitting constants were used to generate computer simulations of the spectra confirming the presence of free radical products.

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