In this study, we investigated the optical features of the redox metal-dependent proteins cytochrome-c, horseradish peroxidase (HRP), and ascorbate oxidase embedded in a sol-gel-processed silica matrix as a function of gelation time. Circular dichroism, absorbance, and fluorescence spectroscopies revealed that the sol-gel process affects the complex structure of the dimeric ascorbate oxidase (although the prosthetic coppers still remain bound to the enzyme) but not that of monomeric cytochrome-e and HRP. Any modifications in ascorbate oxidase occurred in the initial gelation phase; the drying process induced no further alterations and the enzyme remained stable for months. Unfolding-refolding experiments on cytochrome-e revealed severely restricted motility in the protein moiety in the xerogel, the concentrated matrix that forms after drying. The diffusion time of the solvent within the matrix, which regulated the enzyme-substrate reaction rate, depended on the thickness of the monolith, not on the dryness of the specimen.

Savini I., S.R. (1999). Catalytic and spectroscopic properties of cytochrome-c, horseradish peroxidase, and ascorbate oxidase embedded in a sol-gel silica matrix as a function of gelation time. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 82(3), 227-241.

Catalytic and spectroscopic properties of cytochrome-c, horseradish peroxidase, and ascorbate oxidase embedded in a sol-gel silica matrix as a function of gelation time

SAVINI, ISABELLA;SANTUCCI, ROBERTO;DI VENERE, ALMERINDA;ROSATO, NICOLA;AVIGLIANO, LUCIANA
1999

Abstract

In this study, we investigated the optical features of the redox metal-dependent proteins cytochrome-c, horseradish peroxidase (HRP), and ascorbate oxidase embedded in a sol-gel-processed silica matrix as a function of gelation time. Circular dichroism, absorbance, and fluorescence spectroscopies revealed that the sol-gel process affects the complex structure of the dimeric ascorbate oxidase (although the prosthetic coppers still remain bound to the enzyme) but not that of monomeric cytochrome-e and HRP. Any modifications in ascorbate oxidase occurred in the initial gelation phase; the drying process induced no further alterations and the enzyme remained stable for months. Unfolding-refolding experiments on cytochrome-e revealed severely restricted motility in the protein moiety in the xerogel, the concentrated matrix that forms after drying. The diffusion time of the solvent within the matrix, which regulated the enzyme-substrate reaction rate, depended on the thickness of the monolith, not on the dryness of the specimen.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10
eng
Con Impact Factor ISI
ascorbate oxidase; cytochrome c oxidase; horseradish peroxidase; article; circular dichroism; cucumber; enzyme analysis; enzyme mechanism; enzyme modification; nonhuman; oxidation reduction reaction; reaction analysis; spectroscopy; Ascorbate Oxidase; Catalysis; Circular Dichroism; Cytochrome c Group; Horseradish Peroxidase; Kinetics; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Rosales; Silicon Dioxide; Spectrometry, Fluorescence; Time Factors; Armoracia rusticana; Cucumis sativus; Lycaeninae
Savini I., S.R. (1999). Catalytic and spectroscopic properties of cytochrome-c, horseradish peroxidase, and ascorbate oxidase embedded in a sol-gel silica matrix as a function of gelation time. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 82(3), 227-241.
Savini I., Santucci R., Di Venere A., Rosato N., Strukul G., Pinna F., Avigliano L.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/51159
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