Electron-transfer biosensors.

Journal article

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, H2O2 and cholesterol.

Authors: Frew, J; Hill, H

• Publication status: Published
• Journal: Philosophical transactions of the Royal Society of London. Series B, Biological sciences
• Volume: 316
• Issue: 1176
• Pages: 95-106
• Publication date: 1987-08-01
• DOI: 10.1098/rstb.1987.0020
• EISSN: 1471-2970
• ISSN: 0962-8436
• Language: English
• Keywords: Enzymes, Immobilized; Electron Transport; Biotechnology; Cholesterol Oxidase; Oxidation-Reduction; Electrochemistry; Humans; Cholesterol; Proteins