Membrane-entrapped microperoxidase as a 'solid-state' promoter in the electrochemistry of soluble metalloproteins

Immobilization of biological systems in solid matrices is presently of great interest, in view of the many potential advantages associated with both the higher stability of the immobilized macromolecules and the potential utilization for biotechnology. In the present paper the electrochemical behavi...

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Bibliographic Details
Published inBiochemical journal Vol. 264; no. 1; pp. 301 - 304
Main Authors Brunori, M, Santucci, R, Campanella, L, Tranchida, G
Format Journal Article
LanguageEnglish
Published England 15.11.1989
Subjects
Azurin
Cytochrome c Group
Electrochemistry
Electrodes
In Vitro Techniques
Membranes
Metalloproteins
Peptide Fragments
Solubility
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Summary:Immobilization of biological systems in solid matrices is presently of great interest, in view of the many potential advantages associated with both the higher stability of the immobilized macromolecules and the potential utilization for biotechnology. In the present paper the electrochemical behaviour of the undecapeptide from cytochrome c (called microperoxidase) tightly entrapped in cellulose triacetate membrane is reported; its utilization as 'solid-state' promoter in the electrochemistry of soluble metalloproteins is presented. The results obtained indicate that: (i) membrane-entrapped microperoxidase undergoes rapid reversible electron transfer at a glassy carbon electrode; (ii) the electrochemical process is diffusion-controlled; (iii) entrapped microperoxidase acts as 'solid-state' promoter in the electrochemistry of soluble cytochrome c and of azurin.
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj2640301