Immobilization of Bacterial Luciferase into Poly(N-isopropylacrylamide) Film for Electrochemical Control of a Bioluminescence Reaction

A poly(N-isopropylacrylamide) film was modified on an indium-tin oxide electrode in order to immobilize bacterial luciferase (BL) on the electrode surface. By using the modified electrode, flavin mononucleotide (FMN) was electrochemically reduced to FMNH2, which is one of the substrates of the BL lu...

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Bibliographic Details
Published in:Analytical Sciences 2012/10/10, Vol.28(10), pp.1013-1015
Main Authors: KAWANAMI, Yoji, YAMASAKI, Shinya, YAMADA, Shuto, TAKEHARA, Kô
Format: Article
Language:English
Subjects:
Acrylic Resins - chemistry
Aliivibrio fischeri - enzymology
Analytical Chemistry
Bacteria
Bioluminescence
Chemistry
Dodecanol - chemistry
Electrochemistry - methods
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Flavin Mononucleotide - chemistry
Hydrophobic and Hydrophilic Interactions
Luciferases - chemistry
Luciferases - metabolism
Luminescent Measurements - methods
Oxidation-Reduction
Tin Compounds - chemistry
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Summary:A poly(N-isopropylacrylamide) film was modified on an indium-tin oxide electrode in order to immobilize bacterial luciferase (BL) on the electrode surface. By using the modified electrode, flavin mononucleotide (FMN) was electrochemically reduced to FMNH2, which is one of the substrates of the BL luminescence reaction, to control the bioluminescence reaction by BL. The BL reaction in the modified film could be promoted and controlled by the electrochemical generation of FMNH2. This BL luminescence system was evaluated as a model system for the inhibitory assay of hydrophobic molecules on protein functions.
ISSN:0910-6340
1348-2246
DOI:10.2116/analsci.28.1013