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

Patrícia Ferreira, Juan Carro, Beatriz Balcells, Ángel T. Martı́nez, Ana Serrano

2023Applied and Environmental Microbiology20 citationsDOIOpen Access PDF

Abstract

. The results presented, including reactions in the presence of both oxidizing substrates-benzoquinone and molecular oxygen-suggest that such aryl-alcohol dehydrogenase activity, although less important than its oxidase activity in terms of maximal turnover, may have a physiological role during fungal decay of lignocellulose by the reduction of quinones (and phenoxy radicals) from lignin degradation, preventing repolymerization. Moreover, the resulting hydroquinones would participate in redox-cycling reactions for the production of hydroxyl free radical involved in the oxidative attack of the plant cell-wall. Hydroquinones can also act as mediators for laccases and peroxidases in lignin degradation in the form of semiquinone radicals, as well as activators of lytic polysaccharide monooxygenases in the attack of crystalline cellulose. Moreover, reduction of these, and other phenoxy radicals produced by laccases and peroxidases, promotes lignin degradation by limiting repolymerization reactions. These findings expand the role of AAO in lignin biodegradation.

Topics & Concepts

QuinoneOxidizing agentChemistryBenzoquinoneAlcohol dehydrogenaseArylLigninReductaseAlcoholOxygenBiochemistryConiferyl alcoholRadicalDehydrogenaseOxidase testSubstrate (aquarium)EnzymePhotochemistryOrganic chemistryBiologyAlkylEcologyEnzyme-mediated dye degradationPlant Gene Expression AnalysisBiofuel production and bioconversion
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