Here, we describe the electrochemical investigation of hFMO3 in a nano-electrode system, based on AuNPs stabilised with the liquid phase of DDAB on glassy carbon electrodes. In particular, we have studied the electrochemistry of hFMO3 by comparing the redox features of the protein with those of free FAD, both in cyclic voltammetry and in square-wave voltammetry, in the presence and absence of oxygen. Finally, the capability of the immobilised enzyme to turnover a known substrate of hFMO3, benzydamine (nonsteroidal anti-inflammatory drug), was investigated.
Electrochemical investigation of human flavin-containing monooxygenase 3 on nano structured electrodes: Direct electron transfer with stabilised gold nano particles
CASTRIGNANO', SILVIA;SADEGHI, JILA;GILARDI, Gianfranco
2013-01-01
Abstract
Here, we describe the electrochemical investigation of hFMO3 in a nano-electrode system, based on AuNPs stabilised with the liquid phase of DDAB on glassy carbon electrodes. In particular, we have studied the electrochemistry of hFMO3 by comparing the redox features of the protein with those of free FAD, both in cyclic voltammetry and in square-wave voltammetry, in the presence and absence of oxygen. Finally, the capability of the immobilised enzyme to turnover a known substrate of hFMO3, benzydamine (nonsteroidal anti-inflammatory drug), was investigated.File in questo prodotto:
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