PubMed · 4733300
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B Paletta, H Trutnovsky, F Aussenegg, H Gilly. 1973-08-15. [Enzyme reactions studied by laser-interferometry].. https://doi.org/10.1007/bf01930449
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Glucose oxidase mediates the aerobic oxidation of simple sugars to lactones using a noncovalently bound flavin cofactor. The chemical mechanism of this reaction has been uncertain for many years. Here it is shown, using enzymes reconstituted with chemically modified cofactors, that sugar oxidation most likely occurs by concerted hydride (H-) abstraction. Studies of the kinetics and thermodynamics together with the application of Marcus theory reveal a large reorganization energy barrier. The magnitude of this intrinsic contribution appears characteristic of H- transfer in proteins and in solution. The observation that neither the thermodynamics nor reorganization energy is significantly altered in the glucose oxidase active site raises questions concerning how the redox reaction may be catalyzed.
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Silicon nitride (Si3N4) sensing gate pH-ion-selective field effect transistors (ISFETs) were treated by 2.54-GHz microwave O2 plasma, the results show the ISFET sensitivity has an advantage up to 24% increment after the plasma treatment. Electron spectroscopy for chemical analysis (ESCA) is used to make sure that the plasma treatment is not just a native oxide cleaning procedure. The samples, which were immobilized with glutaraldehyde used as a bifunctional reagent and 3-aminopropyItriethoxysilane used as an adhesion promoter were studied. The binding force between the glucose oxidase and glutaraldehyde immobilized samples, and the element concentrations of nitrogen in 3-aminopropyltriethoxysilane immobilized samples are higher which were treated by plasma.