Abstract
The electrochemistry of redox proteins is now well established. Conditions exist which allow electron-transfer reactions of all simple proteins to proceed rapidly and reversibly at electrodes. Coupling of the electrode reaction to enzymes, for which the redox proteins act as cofactors, allows exploitation of this good electrochemistry. This is well illustrated by the enzyme-catalysed electrochemical oxidation of
p
-cresol to
p
-hydroxybenzaldehyde, which has been shown to proceed along with coupling to the electrode via the copper protein, azurin, or the organometallic compound ferroceneboronic acid. Ferrocene derivatives, in general, show a degree of versatility, coupling the electron-transfer reactions of many enzymes. Thus derivatives of the ferricinium ion act as excellent electron-transfer reagents from the enzyme glucose oxidase. The system is capable of detecting glucose in blood. Similar procedures, in conjunction with the appropriate enzyme, have yielded assays for, among others, H
2
O
2
and cholesterol.
Subject
Industrial and Manufacturing Engineering,General Agricultural and Biological Sciences,General Business, Management and Accounting,Materials Science (miscellaneous),Business and International Management
Reference21 articles.
1. Albery W .J. 1975 Electrode kinetics. Oxford: Clarendon Press.
2. Mechanism of the reduction and oxidation reactions of cytochrome cat a modified gold electrode. chem;Albery Wr. J.;Soc.,1981
3. Surface modifiers for the promotion of direct electrochemistry of cytochrome c. J .electroanalyt;Allen P. M.;Chem.,1984
4. Direct electrochemical reduction of ferredoxin promoted by Mg2+
5. Surface selectivity in the direct electrochemistry of redox proteins. Contrasting behaviour at edge and basal planes of graphite
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