ArticleBiochemistry2013
Oxidation mode of pyranose 2-oxidase is controlled by pH.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Identification of a robust bacterial pyranose oxidase that displays an unusual pH dependence.The Journal of biological chemistry · 2024Article
- Tunable Properties of Nature-InspiredMolecules (Basel, Switzerland) · 2020Article
- Characterization of pyranose oxidase variants for bioelectrocatalytic applications.Biochimica et biophysica acta. Proteins and proteomics · 2020Article
- Degradation of bamboo lignocellulose by bamboo snout beetleBiotechnology for biofuels · 2019Article
- Novel Riboflavin-Inspired Conjugated Bio-Organic Semiconductors.Molecules (Basel, Switzerland) · 2018Article
- De novo transcriptome assembly of the bamboo snout beetleBiotechnology for biofuels · 2018Article
- Electrochemical characterization of the pyranose 2-oxidase variant N593C shows a complete loss of the oxidase function with full preservation of substrate (dehydrogenase) activity.Physical chemistry chemical physics : PCCP · 2016Article
- Genomic and secretomic insight into lignocellulolytic system of an endophytic bacterium Pantoea ananatis Sd-1.Biotechnology for biofuels · 2016Article
- Article
- Crystal structures of Phanerochaete chrysosporium pyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assembly.FEBS open bio · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Pyranose 2-oxidase (P2O) from Trametes multicolor is a flavoenzyme that catalyzes the oxidation of d-glucose and other aldopyranose sugars at the C2 position by using O₂ as an electron acceptor to form the corresponding 2-keto-sugars and H₂O₂. In this study, the effects of pH on the oxidative half-reaction of P2O were investigated using stopped-flow spectrophotometry. The results showed that flavin oxidation occurred via different pathways depending on the pH of the environment. At pH values lower than 8.0, reduced P2O reacts with O₂ to form a C4a-hydroperoxyflavin intermediate, leading to elimination of H₂O₂. At pH 8.0 and higher, the majority of the reduced P2O reacts with O₂ via a pathway that does not allow detection of the C4a-hydroperoxyflavin, and flavin oxidation occurs with decreased rate constants upon the rise in pH. The switching between the two modes of P2O oxidation is controlled by protonation of a group which has a pK(a) of 7.6 ± 0.1. Oxidation reactions of reduced P2O under rapid pH change as performed by stopped-flow mixing were different from the same reactions performed with enzyme pre-equilibrated at the same specified pH values, implying that the protonation of the group which controls the mode of flavin oxidation cannot be rapidly equilibrated with outside solvent. Using a double-mixing stopped-flow experiment, a rate constant for proton dissociation from the reaction site was determined to be 21.0 ± 0.4 s⁻¹.
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Registered trials
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