Electrochemistry of the flavodehydrogenase domain of flavocytochrome b(2) engineered for L-mandelate dehydrogenase activity

Huihong Liu, H. Allen O. Hill, SK Chapman

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    6 Citations (Scopus)

    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 languageEnglish
    Pages (from-to)598-603
    Number of pages6
    JournalJournal of Electroanalytical Chemistry and Interfacial Electrochemistry
    Volume500
    Issue number1-2
    DOIs
    Publication statusPublished - 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

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