Reagentless Mediated Laccase Electrode for the Detection of Enzyme Modulators

Francis Trudeau; Francis Daigle; Dónal Leech

doi:10.1021/ac960554d

Reagentless Mediated Laccase Electrode for the Detection of Enzyme Modulators

Francis Trudeau, Francis Daigle, Dónal Leech

Université de Montréal

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

88 Citations (Scopus)

Abstract

We have investigated aerobic mediation of electron transfer to a laccase enzyme by the solution redox couples [Os(bpy)₂Cl₂]^+/0 and [Os(bpy)₂(MeIm)Cl]^2+/+, where bpy is 2,2-bipyridine and MeIm is N-methylimidazole. The factors that influence the homogeneous mediation reaction are investigated and discussed. Investigation of ionic strength, pH, and temperature effects on the kinetics of intermolecular electron transfer elucidates the governing factors in the mediator - enzyme reactions. Coimmobilization of both enzyme and an osmium redox mediator in a hydrogel on glassy carbon electrodes results in a biosensor for the reagentless addressing of enzyme activity, consuming only oxygen present in solution. Thus, these immobilized enzyme biosensors can be utilized for the detection of modulators of laccase activity, such as the inhibitor sodium azide. The enzyme inhibition biosensor can detect levels of azide as low as 2.5 × 10^-6 mol dm^-3 in solution.

Original language	English
Pages (from-to)	882-886
Number of pages	5
Journal	Analytical Chemistry
Volume	69
Issue number	5
DOIs	https://doi.org/10.1021/ac960554d
Publication status	Published - 1997
Externally published	Yes

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title = "Reagentless Mediated Laccase Electrode for the Detection of Enzyme Modulators",

abstract = "We have investigated aerobic mediation of electron transfer to a laccase enzyme by the solution redox couples [Os(bpy)2Cl2]+/0 and [Os(bpy)2(MeIm)Cl]2+/+, where bpy is 2,2-bipyridine and MeIm is N-methylimidazole. The factors that influence the homogeneous mediation reaction are investigated and discussed. Investigation of ionic strength, pH, and temperature effects on the kinetics of intermolecular electron transfer elucidates the governing factors in the mediator - enzyme reactions. Coimmobilization of both enzyme and an osmium redox mediator in a hydrogel on glassy carbon electrodes results in a biosensor for the reagentless addressing of enzyme activity, consuming only oxygen present in solution. Thus, these immobilized enzyme biosensors can be utilized for the detection of modulators of laccase activity, such as the inhibitor sodium azide. The enzyme inhibition biosensor can detect levels of azide as low as 2.5 × 10-6 mol dm-3 in solution.",

author = "Francis Trudeau and Francis Daigle and D{\'o}nal Leech",

year = "1997",

doi = "10.1021/ac960554d",

language = "English",

volume = "69",

pages = "882--886",

journal = "Analytical Chemistry",

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publisher = "American Chemical Society",

number = "5",

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TY - JOUR

T1 - Reagentless Mediated Laccase Electrode for the Detection of Enzyme Modulators

AU - Trudeau, Francis

AU - Daigle, Francis

AU - Leech, Dónal

PY - 1997

Y1 - 1997

N2 - We have investigated aerobic mediation of electron transfer to a laccase enzyme by the solution redox couples [Os(bpy)2Cl2]+/0 and [Os(bpy)2(MeIm)Cl]2+/+, where bpy is 2,2-bipyridine and MeIm is N-methylimidazole. The factors that influence the homogeneous mediation reaction are investigated and discussed. Investigation of ionic strength, pH, and temperature effects on the kinetics of intermolecular electron transfer elucidates the governing factors in the mediator - enzyme reactions. Coimmobilization of both enzyme and an osmium redox mediator in a hydrogel on glassy carbon electrodes results in a biosensor for the reagentless addressing of enzyme activity, consuming only oxygen present in solution. Thus, these immobilized enzyme biosensors can be utilized for the detection of modulators of laccase activity, such as the inhibitor sodium azide. The enzyme inhibition biosensor can detect levels of azide as low as 2.5 × 10-6 mol dm-3 in solution.

AB - We have investigated aerobic mediation of electron transfer to a laccase enzyme by the solution redox couples [Os(bpy)2Cl2]+/0 and [Os(bpy)2(MeIm)Cl]2+/+, where bpy is 2,2-bipyridine and MeIm is N-methylimidazole. The factors that influence the homogeneous mediation reaction are investigated and discussed. Investigation of ionic strength, pH, and temperature effects on the kinetics of intermolecular electron transfer elucidates the governing factors in the mediator - enzyme reactions. Coimmobilization of both enzyme and an osmium redox mediator in a hydrogel on glassy carbon electrodes results in a biosensor for the reagentless addressing of enzyme activity, consuming only oxygen present in solution. Thus, these immobilized enzyme biosensors can be utilized for the detection of modulators of laccase activity, such as the inhibitor sodium azide. The enzyme inhibition biosensor can detect levels of azide as low as 2.5 × 10-6 mol dm-3 in solution.

UR - https://www.scopus.com/pages/publications/0001692370

U2 - 10.1021/ac960554d

DO - 10.1021/ac960554d

M3 - Article

SN - 0003-2700

VL - 69

SP - 882

EP - 886

JO - Analytical Chemistry

JF - Analytical Chemistry

IS - 5

ER -

Reagentless Mediated Laccase Electrode for the Detection of Enzyme Modulators

Abstract

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