Voltammetric behavior of dihydronicotinamide adenine dinucleotide phosphate at enzyme-modified electrodes

✍ Scribed by Chi Hua; Sean Walsh; Malcolm R. Smyth; Ivan Švancara; Karel Vytřas

• Book ID: 102183236
• Publisher: John Wiley and Sons
• Year: 1992
• Tongue: English
• Weight: 288 KB
• Volume: 4
• Category: Article
• ISSN: 1040-0397
• DOI: 10.1002/elan.1140040119

✦ Synopsis

The oxidation o f nicotinamide-adenine dinucleotide phosphate (reduced form, NADPH) at glassy carbon electrodes modified with different enzymes has been studied. It was found that NADPH yielded a well-defined anodic peak about + 0.70 V (vs. Ag/AgCI) at glassy carbon electrodes coated with three different enzymes, glutathione reductase, glutathione peroxidase, and glucose oxidase, in 1.4 M potassium phosphate supporting electrolyte. It was confirmed that the enzymes immobilized at the working electrode surface reduced the overpotential for the oxidation of NADPH. This method provides a way to study the mechanism of some enzyniatic reactions.