Expanding the Physiological Role of Aryl-Alcohol Flavooxidases as Quinone Reductases

• Published in: Applied and environmental microbiology Vol. 89; no. 5; p. e0184422
• Main Authors: Ferreira, Patricia, Carro, Juan, Balcells, Beatriz, Martínez, Angel T., Serrano, Ana
• Format: Journal Article
• Language: English
• Published: United States American Society for Microbiology 31.05.2023
• Subjects: Alcohol oxidase; Alcohol Oxidoreductases - metabolism; Alcohols; Aldehydes; Aromatic compounds; Benzoquinone; Benzoquinones; Choline; Choline oxidase; Degradation; Dichlorophenolindophenol; E coli; Environmental Microbiology; Enzymes; Ethanol; Flavoproteins; Hydrogen Peroxide; Hydroquinones; Lignin; Lignin - metabolism; Metabolites; Oxidation; Peroxidases - genetics; Phenolic compounds; Phenols; Physicochemical properties; Pleurotus - metabolism; Quinone Reductases; Quinones; Reductases; Secondary metabolites; Substrate specificity; Substrates; White rot; Pleurotus AAO; Bjerkandera adusta AAO; flavooxidases; lignocellulose decay; aryl-alcohol oxidase (AAO); heterologous expression; quinone reduction; GMC superfamily

In this work, quinone reductase activity is analyzed in three AAO flavooxidases, whose preferred oxidizing-substrate is O 2 . The results presented, including reactions in the presence of both oxidizing substrates—benzoquinone and molecular oxygen—suggest that such aryl-alcohol dehydrogenase activit...