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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2008
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15675394_v74_n1_p201_Flexer http://hdl.handle.net/20.500.12110/paper_15675394_v74_n1_p201_Flexer |
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paper:paper_15675394_v74_n1_p201_Flexer2023-06-08T16:24:06Z Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations 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. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15675394_v74_n1_p201_Flexer 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 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. |
| 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 |
| publishDate |
2008 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15675394_v74_n1_p201_Flexer http://hdl.handle.net/20.500.12110/paper_15675394_v74_n1_p201_Flexer |
| _version_ |
1768542195849101312 |