Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations

The homogeneous reaction between glucose oxidase and osmium bipyridine-pyridine carboxylic acid in the presence of glucose has been studied in detail by cyclic voltammetry and digital simulation. Combination of the analytical equations that describe the dependence of the amperometric response on enz...

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Autores principales: Flexer, V., Ielmini, M.V., Calvo, E.J., Bartlett, P.N.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_15675394_v74_n1_p201_Flexer
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spelling todo:paper_15675394_v74_n1_p201_Flexer2023-10-03T16:26:40Z Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations Flexer, V. Ielmini, M.V. Calvo, E.J. Bartlett, P.N. Enzyme electrode Glucose oxidase Kinetics Mediator Osmium bipyridine Acids Carboxylic acids Digital arithmetic Electrolysis Enzymes Glucose Glucose oxidase Glucose sensors Kinetic parameters Organic acids Osmium Substrates Voltammetry Accurate Amperometric responses Analytical equations Bipyridine Bulk solutions Digital simulations Electrode surfaces Enzyme electrode Enzyme reactions Homogeneous reactions Limiting cases Mediator Pyridine carboxylic acids Redox mediators Reduced forms Substrate concentrations Cyclic voltammetry carboxylic acid glucose oxidase osmium pyridine amperometry article catalysis chemical structure cyclic potentiometry diffusion electrochemistry electrode enzyme inactivation enzyme kinetics enzyme mechanism enzyme substrate oxidation reduction reaction simulation Electrochemistry Enzyme Activation Glucose Oxidase Kinetics Organometallic Compounds Osmium Oxidation-Reduction The homogeneous reaction between glucose oxidase and osmium bipyridine-pyridine carboxylic acid in the presence of glucose has been studied in detail by cyclic voltammetry and digital simulation. Combination of the analytical equations that describe the dependence of the amperometric response on enzyme, substrate and co-substrate concentrations for the limiting cases with digital simulation of the coupled enzyme reaction diffusion problem allows us to extract kinetic parameters for the substrate-enzyme reaction: KMS = 10.8 mM, kcat = 254 s- 1 and for the redox mediator-enzyme reaction, k = 2.2 × 105 M- 1 s- 1. The accurate determination of the kinetic parameters at low substrate concentrations (< 7 mM) is limited by depletion of the substrate close to the electrode surface. At high substrate concentrations (> 20 mM) inactivation of the reduced form of glucose oxidase in the bulk solution must be taken into account in the analysis of the results. © 2008 Elsevier B.V. All rights reserved. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_15675394_v74_n1_p201_Flexer
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Enzyme electrode
Glucose oxidase
Kinetics
Mediator
Osmium bipyridine
Acids
Carboxylic acids
Digital arithmetic
Electrolysis
Enzymes
Glucose
Glucose oxidase
Glucose sensors
Kinetic parameters
Organic acids
Osmium
Substrates
Voltammetry
Accurate
Amperometric responses
Analytical equations
Bipyridine
Bulk solutions
Digital simulations
Electrode surfaces
Enzyme electrode
Enzyme reactions
Homogeneous reactions
Limiting cases
Mediator
Pyridine carboxylic acids
Redox mediators
Reduced forms
Substrate concentrations
Cyclic voltammetry
carboxylic acid
glucose oxidase
osmium
pyridine
amperometry
article
catalysis
chemical structure
cyclic potentiometry
diffusion
electrochemistry
electrode
enzyme inactivation
enzyme kinetics
enzyme mechanism
enzyme substrate
oxidation reduction reaction
simulation
Electrochemistry
Enzyme Activation
Glucose Oxidase
Kinetics
Organometallic Compounds
Osmium
Oxidation-Reduction
spellingShingle Enzyme electrode
Glucose oxidase
Kinetics
Mediator
Osmium bipyridine
Acids
Carboxylic acids
Digital arithmetic
Electrolysis
Enzymes
Glucose
Glucose oxidase
Glucose sensors
Kinetic parameters
Organic acids
Osmium
Substrates
Voltammetry
Accurate
Amperometric responses
Analytical equations
Bipyridine
Bulk solutions
Digital simulations
Electrode surfaces
Enzyme electrode
Enzyme reactions
Homogeneous reactions
Limiting cases
Mediator
Pyridine carboxylic acids
Redox mediators
Reduced forms
Substrate concentrations
Cyclic voltammetry
carboxylic acid
glucose oxidase
osmium
pyridine
amperometry
article
catalysis
chemical structure
cyclic potentiometry
diffusion
electrochemistry
electrode
enzyme inactivation
enzyme kinetics
enzyme mechanism
enzyme substrate
oxidation reduction reaction
simulation
Electrochemistry
Enzyme Activation
Glucose Oxidase
Kinetics
Organometallic Compounds
Osmium
Oxidation-Reduction
Flexer, V.
Ielmini, M.V.
Calvo, E.J.
Bartlett, P.N.
Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations
topic_facet Enzyme electrode
Glucose oxidase
Kinetics
Mediator
Osmium bipyridine
Acids
Carboxylic acids
Digital arithmetic
Electrolysis
Enzymes
Glucose
Glucose oxidase
Glucose sensors
Kinetic parameters
Organic acids
Osmium
Substrates
Voltammetry
Accurate
Amperometric responses
Analytical equations
Bipyridine
Bulk solutions
Digital simulations
Electrode surfaces
Enzyme electrode
Enzyme reactions
Homogeneous reactions
Limiting cases
Mediator
Pyridine carboxylic acids
Redox mediators
Reduced forms
Substrate concentrations
Cyclic voltammetry
carboxylic acid
glucose oxidase
osmium
pyridine
amperometry
article
catalysis
chemical structure
cyclic potentiometry
diffusion
electrochemistry
electrode
enzyme inactivation
enzyme kinetics
enzyme mechanism
enzyme substrate
oxidation reduction reaction
simulation
Electrochemistry
Enzyme Activation
Glucose Oxidase
Kinetics
Organometallic Compounds
Osmium
Oxidation-Reduction
description The homogeneous reaction between glucose oxidase and osmium bipyridine-pyridine carboxylic acid in the presence of glucose has been studied in detail by cyclic voltammetry and digital simulation. Combination of the analytical equations that describe the dependence of the amperometric response on enzyme, substrate and co-substrate concentrations for the limiting cases with digital simulation of the coupled enzyme reaction diffusion problem allows us to extract kinetic parameters for the substrate-enzyme reaction: KMS = 10.8 mM, kcat = 254 s- 1 and for the redox mediator-enzyme reaction, k = 2.2 × 105 M- 1 s- 1. The accurate determination of the kinetic parameters at low substrate concentrations (< 7 mM) is limited by depletion of the substrate close to the electrode surface. At high substrate concentrations (> 20 mM) inactivation of the reduced form of glucose oxidase in the bulk solution must be taken into account in the analysis of the results. © 2008 Elsevier B.V. All rights reserved.
format JOUR
author Flexer, V.
Ielmini, M.V.
Calvo, E.J.
Bartlett, P.N.
author_facet Flexer, V.
Ielmini, M.V.
Calvo, E.J.
Bartlett, P.N.
author_sort Flexer, V.
title Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations
title_short Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations
title_full Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations
title_fullStr Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations
title_full_unstemmed Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations
title_sort extracting kinetic parameters for homogeneous [os(bpy)2clpycooh]+ mediated enzyme reactions from cyclic voltammetry and simulations
url http://hdl.handle.net/20.500.12110/paper_15675394_v74_n1_p201_Flexer
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