Voltammetric behavior of dihydronicotinamide adenine dinucleotide phosphate at enzyme‐modified electrodes | Zendy

Hua Chi | Zendy; Walsh Sean | Zendy; Smyth Malcolm R. | Zendy; Švancara Ivan | Zendy; Vytřas Karel | Zendy

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

Author(s) -

Hua Chi,

Walsh Sean,

Smyth Malcolm R.,

Švancara Ivan,

Vytřas Karel

Publication year - 1992

Publication title -

electroanalysis

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.574

H-Index - 128

eISSN - 1521-4109

pISSN - 1040-0397

DOI - 10.1002/elan.1140040119

Subject(s) - nicotinamide adenine dinucleotide phosphate , chemistry , overpotential , glutathione reductase , inorganic chemistry , potassium phosphate , glassy carbon , phosphate , nicotinamide adenine dinucleotide , glucose oxidase , electrode , enzyme , glutathione , glutathione peroxidase , oxidase test , electrochemistry , biochemistry , nad+ kinase , cyclic voltammetry , organic chemistry

The oxidation of 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/AgCl) 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 enzymatic reactions.

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