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Electro-catalysis by immobilised human flavin-containing monooxygenase isoform 3 (hFMO3).
- Source :
-
Analytical & Bioanalytical Chemistry . Oct2010, Vol. 398 Issue 3, p1403-1409. 7p. 1 Diagram, 2 Charts, 3 Graphs. - Publication Year :
- 2010
-
Abstract
- Human flavin-containing monooxygenases are the second most important class of drug-metabolizing enzymes after cytochromes P450. Here we report a simple but functional and stable enzyme-electrode system based on a glassy carbon (GC) electrode with human flavin-containing monooxygenase isoform 3 (hFMO3) entrapped in a gel cross-linked with bovine serum albumin (BSA) by glutaraldehyde. The enzymatic electrochemical responsiveness is characterised by using well-known substrates: trimethylamine (TMA), ammonia (NH), triethylamine (TEA), and benzydamine (BZD). The apparent Michaelis–Menten constant ( K′) and apparent maximum current ( I′) are calculated by fitting the current signal to the Michaelis–Menten equation for each substrate. The enzyme-electrode has good characteristics: the calculated sensitivity was 40.9 ± 0.5 mA mol L cm for TMA, 43.3 ± 0.1 mA mol L cm for NH, 45.2 ± 2.2 mA mol L cm for TEA, and 39.3 ± 0.6 mA mol L cm for BZD. The stability was constant for 3 days and the inter-electrode reproducibility was 12.5%. This is a novel electrochemical tool that can be used to investigate new potential drugs against the catalytic activity of hFMO3. [ABSTRACT FROM AUTHOR]
- Subjects :
- *MONOOXYGENASES
*OXYGENASES
*FLAVINS
*COENZYMES
*CYTOCHROMES
Subjects
Details
- Language :
- English
- ISSN :
- 16182642
- Volume :
- 398
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Analytical & Bioanalytical Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 53476283
- Full Text :
- https://doi.org/10.1007/s00216-010-4014-z