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Titel
Electrochemical characterization of the pyranose 2-oxidase variant N593C shows a complete loss of the oxidase function with full preservation of substrate (dehydrogenase) activity
VerfasserBrugger, Dagmar ; Sützl, Leander ; Zahma, Kawah ; Haltrich, Dietmar ; Peterbauer, Clemens K. ; Stoica, Leonard
Erschienen in
Physical Chemistry Chemical Physics, London, 2016, Jg. 18, S. 32072-32077
ErschienenRoyal Society of Chemistry, 2016
SpracheEnglisch
DokumenttypAufsatz in einer Zeitschrift
Schlagwörter (DE)nicht verfügbar
ISSN1463-9084
URNurn:nbn:at:at-ubbw:3-1938 Persistent Identifier (URN)
DOI10.1039/C6CP06009A 
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 Das Werk ist frei verfügbar
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Electrochemical characterization of the pyranose 2-oxidase variant N593C shows a complete loss of the oxidase function with full preservation of substrate (dehydrogenase) activity [2.13 mb]
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Zusammenfassung (Englisch)

This study presents the first electrochemical characterization of the pyranose oxidase (POx) variant N593C (herein called POx-C), which is considered a promising candidate for future glucose-sensing applications. The resulting cyclic voltammograms obtained in the presence of various concentrations of glucose and mediator (1,4-benzoquinone, BQ), as well as the control experiments by addition of catalase, support the conclusion of a complete suppression of the oxidase function and oxygen reactivity at POx-C. Additionally, these electrochemical experiments demonstrate, contrary to previous biochemical studies, that POx-C has a fully retained enzymatic activity towards glucose. POx-C was immobilized on a special screen-printed electrode (SPE) based on carbon ink and grafted with gold-nanoparticles (GNP). Suppression of the oxygen reactivity at N593C-POx variant is a prerequisite for utilizing POx in electrochemical applications for glucose sensing. To our knowledge, this is the first report presented in the literature showing an absolute conversion of an oxidase into a fully active equivalent dehydrogenase via a single residue exchange.

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