Use of solid-state promoters in the electrochemistry of cytochrome c at a gold electrode

The direct electrochemistry of cytochrome c at a gold electrode was investigated by cyclic voltammetry using, as promoters, microperoxidase (the haem-undecapeptide obtained by hydrolysis of cytochrome c), Fe(III)-protoporphyrin IX or protoporphyrin-IX, all entrapped in a cellulose triacetate membran...

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Published inBiochemical journal Vol. 273; no. 3; pp. 783 - 786
Main Authors SANTUCCI, R, FARAONI, A, CAMPANELLA, L, TRANCHIDA, G, BRUNORI, M
Format Journal Article
LanguageEnglish
Published Colchester Portland Press 01.02.1991
Subjects
Animals
Biological and medical sciences
Cytochrome c Group - metabolism
Electrochemistry
Electrodes
Electron Transport
Enzymes, Immobilized - metabolism
Fundamental and applied biological sciences. Psychology
Gold
Horses
Molecular biophysics
Peroxidases - metabolism
Physical chemistry in biology
Cytochrome c
Promoter
Cyclic voltammetry
Membrane electrode
Hemoprotein
Protoporphyrin
Electrochemistry
Electron transfer
Mechanism of action
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Summary:The direct electrochemistry of cytochrome c at a gold electrode was investigated by cyclic voltammetry using, as promoters, microperoxidase (the haem-undecapeptide obtained by hydrolysis of cytochrome c), Fe(III)-protoporphyrin IX or protoporphyrin-IX, all entrapped in a cellulose triacetate membrane. The results indicate that these immobilized systems strongly enhance the rate of electron transfer between the protein in solution and the electrode surface, and thus behave as 'solid-state' promoters, though with differing efficiencies. These results are of interest because they raise the possibility of engineering an efficient and versatile promoter active also at inert electrode surfaces.
Bibliography:ObjectType-Article-1
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj2730783