Abstract
A ferrocene with double long chains, 2C16GluFc, was synthesized and mediated electron transfer reactions of glucose oxidase, immobilized on a lipid cast film containing the ferrocene, were examined. A basal plane pyrolytic graphite (BPG) electrode modified with a cast of 2C16GluFc and a synthetic lipid, dihexsdecyldimethylammonium bromide (2C16N+Br-) gave phase transition dependent cyclic voltammograms. Normal pulse voltammetry proved that the enhancement of the faradaic current at the electrode at temperatures above the phase transition is ascribable to the increase in the apparent diffusion rate constants. Glucose oxidase was immobilized on the cast film of 2C16GluFc/2C16N+Br- on BPG and ferrocene-mediated catalytic electron transfer reactions in the presence of glucose were explored. Temperature experiments have revealed that the tuning of the lipid bilayer fluidity between crystal-to-liquid crystalline phase regulates the catalytic electron transfer reaction.
| Original language | English |
|---|---|
| Pages (from-to) | 59-62 |
| Number of pages | 4 |
| Journal | Bioelectrochemistry and Bioenergetics |
| Volume | 42 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Apr 1 1997 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Physical and Theoretical Chemistry
- Electrochemistry
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Tuning of lipid bilayer fluidity regulates mediated electron transfer reactions of glucose oxidase immobilized on lipid bilayer films on an electrode. / Tominaga, Masato; Kusano, Satoko; Nakashima, Naotoshi.
In: Bioelectrochemistry and Bioenergetics, Vol. 42, No. 1, 01.04.1997, p. 59-62.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Tuning of lipid bilayer fluidity regulates mediated electron transfer reactions of glucose oxidase immobilized on lipid bilayer films on an electrode
AU - Tominaga, Masato
AU - Kusano, Satoko
AU - Nakashima, Naotoshi
PY - 1997/4/1
Y1 - 1997/4/1
N2 - A ferrocene with double long chains, 2C16GluFc, was synthesized and mediated electron transfer reactions of glucose oxidase, immobilized on a lipid cast film containing the ferrocene, were examined. A basal plane pyrolytic graphite (BPG) electrode modified with a cast of 2C16GluFc and a synthetic lipid, dihexsdecyldimethylammonium bromide (2C16N+Br-) gave phase transition dependent cyclic voltammograms. Normal pulse voltammetry proved that the enhancement of the faradaic current at the electrode at temperatures above the phase transition is ascribable to the increase in the apparent diffusion rate constants. Glucose oxidase was immobilized on the cast film of 2C16GluFc/2C16N+Br- on BPG and ferrocene-mediated catalytic electron transfer reactions in the presence of glucose were explored. Temperature experiments have revealed that the tuning of the lipid bilayer fluidity between crystal-to-liquid crystalline phase regulates the catalytic electron transfer reaction.
AB - A ferrocene with double long chains, 2C16GluFc, was synthesized and mediated electron transfer reactions of glucose oxidase, immobilized on a lipid cast film containing the ferrocene, were examined. A basal plane pyrolytic graphite (BPG) electrode modified with a cast of 2C16GluFc and a synthetic lipid, dihexsdecyldimethylammonium bromide (2C16N+Br-) gave phase transition dependent cyclic voltammograms. Normal pulse voltammetry proved that the enhancement of the faradaic current at the electrode at temperatures above the phase transition is ascribable to the increase in the apparent diffusion rate constants. Glucose oxidase was immobilized on the cast film of 2C16GluFc/2C16N+Br- on BPG and ferrocene-mediated catalytic electron transfer reactions in the presence of glucose were explored. Temperature experiments have revealed that the tuning of the lipid bilayer fluidity between crystal-to-liquid crystalline phase regulates the catalytic electron transfer reaction.
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U2 - 10.1016/S0302-4598(96)05139-2
DO - 10.1016/S0302-4598(96)05139-2
M3 - Article
VL - 42
SP - 59
EP - 62
JO - Bioelectrochemistry
JF - Bioelectrochemistry
SN - 1567-5394
IS - 1
ER -