Abstract
The direct electrochemistry of the flavodehydrogenase domain of flavocytochrome b(2) engineered for L-mandelate dehydrogenase activity (FDH) has been investigated at an edge-plane pyrolytic graphite (EPG) electrode using poly-L-lysine as a promoter. Two redox couples (- 0.481 and - 0.605 V vs. SCE in Tris buffer solution at pH 7.5, scan rate 20 mV s(-1)) were obtained on the cyclic voltammogram which correspond to the separated two peaks in the one-electron reduction-reoxidation steps of enzyme bounded flavin mononucleotide (FMN). The electrochemical transformation of the substrate L-mandelic acid (LMA), catalysed by the FMN-domain of L-mandelate dehydrogenase (LMDH) is inhibited at bare or promoter-modified EPG, but both ferrocenemonocarboxylic acid (FMCA) and cytochrome c function as mediators. (C) 2001 Elsevier Science B.V. All rights reserved.
Original language | English |
---|---|
Pages (from-to) | 598-603 |
Number of pages | 6 |
Journal | Journal of Electroanalytical Chemistry and Interfacial Electrochemistry |
Volume | 500 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 16 Mar 2001 |
Keywords
- ION
- L-mandelate dehydrogenase
- FLAVIN
- REDOX PROTEINS
- FINITE DIFFUSION SPACE
- PYROLYTIC-GRAPHITE ELECTRODES
- edge-plane pyrolytic graphite electrode
- CYTOCHROME-C
- LINEAR SWEEP VOLTAMMETRY
- DIRECT ELECTRON-TRANSFER
- electrochemistry