Electrochemical property of L-mandalate dehydrogenase

Huihong Liu, H A O Hill, Stephen K Chapman

    Research output: Contribution to journalArticle

    Abstract

    The direct electrochemistry of flavodehydrogenase domain (FDH) an genetically engineered enzyme, has been investigated at edge-plane pyrolytic graphite (EPG) electrode using poly-L-lysine as a promoter. Two redox couples (-0.481 V and -0.605 V vs SCE in the tris buffer solution at pH 7.5, scan rate 20 mV/s) were obtained on the cyclic voltammogram which respond to the separated two peaks in 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-fragment of L-mandalate dehydrogenase (LMDH) is inhibited at bare or promoter-modified EPG, but both ferrocenemonocarboxylic acid (FMCA) and cytochrome C, function as mediators.

    Original languageEnglish
    Pages (from-to)755-759
    Number of pages5
    JournalChinese Journal of Analytical Chemistry
    Volume29
    Issue number7
    Publication statusPublished - Jul 2001

    Keywords

    • genetically engineered enzyme
    • ION
    • L-mandalate dehydrogenase
    • PROTEINS
    • CYTOCHROME-C
    • electrochemistry
    • COMPLEXES

    Cite this

    Liu, H., Hill, H. A. O., & Chapman, S. K. (2001). Electrochemical property of L-mandalate dehydrogenase. Chinese Journal of Analytical Chemistry, 29(7), 755-759.