Human sulfite oxidase (hSO) was immobilised on SAM-coated silver electrodes under preservation of the native heme pocket structure of the cytochrome b5 (Cyt b5) domain and the functionality of the enzyme. The redox properties and catalytic activity of the entire enzyme were studied by surface enhanced resonance Raman (SERR) spectroscopy and cyclic voltammetry (CV) and compared to the isolated heme domain when possible. It is shown that heterogeneous electron transfer and catalytic activity of hSO sensitively depend on the local environment of the enzyme.
View Article and Find Full Text PDFAn efficient electrocatalytic biosensor for sulfite detection was developed by co-immobilizing sulfite oxidase and cytochrome c with polyaniline sulfonic acid in a layer-by-layer assembly. QCM, UV-Vis spectroscopy and cyclic voltammetry revealed increasing loading of electrochemically active protein with the formation of multilayers. The sensor operates reagentless at low working potential.
View Article and Find Full Text PDFAn electrocatalytically functional multilayer has been designed using two proteins, cytochrome c and sulfite oxidase, and a polyelectrolyte (polyaniline sulfonate). The two proteins were co-immobilized on the surface of a gold electrode in alternating layers by electrostatic interactions using the layer-by-layer technique. The formation of this fully electro-active multilayer is characterized by quartz crystal microbalance and electrochemical experiments.
View Article and Find Full Text PDFAdv Biochem Eng Biotechnol
February 2008
Electrochemistry using direct electron transfer between an electrode and a protein or an enzyme has developed into a means for studying biological redox reactions and for bioanalytics, biosynthesis and bioenergetics. This review summarizes recent work on direct protein electrochemistry with special emphasis on our results in bioelectrocatalysis using isolated enzymes and enzyme-protein couples.
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