Electrochemistry of the flavodehydrogenase domain of flavocytochrome b2 engineered for l-mandelate dehydrogenase activity
| Autor: | Stephen K Chapman, Huihong Liu, H. Allen O. Hill |
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| Rok vydání: | 2001 |
| Předmět: |
Tris
medicine.medical_specialty biology Immobilized enzyme Stereochemistry General Chemical Engineering Flavoprotein Flavin mononucleotide Dehydrogenase Buffer solution Flavin group Analytical Chemistry chemistry.chemical_compound chemistry Bioelectrochemistry Electrochemistry biology.protein medicine |
| Zdroj: | Journal of Electroanalytical Chemistry. 500:598-603 |
| ISSN: | 1572-6657 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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