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

Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations
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 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 × 10^5 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.

enzyme electrode, mediator, kinetics, glucose oxidase, osmium bipyridine
201-209
Flexer, V.
da447235-0802-405a-876a-02d918abf2ab
Ielmini, M.V.
a384be8f-be81-4550-89d2-7745d8b0b2e3
Calvo, E.J.
66bc120f-b6c6-4f83-af3b-74dbafce0118
Bartlett, P.N.
d99446db-a59d-4f89-96eb-f64b5d8bb075
Flexer, V.
da447235-0802-405a-876a-02d918abf2ab
Ielmini, M.V.
a384be8f-be81-4550-89d2-7745d8b0b2e3
Calvo, E.J.
66bc120f-b6c6-4f83-af3b-74dbafce0118
Bartlett, P.N.
d99446db-a59d-4f89-96eb-f64b5d8bb075

Flexer, V., Ielmini, M.V., Calvo, E.J. and Bartlett, P.N. (2008) Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations. Bioelectrochemistry, 74 (1), 201-209. (doi:10.1016/j.bioelechem.2008.08.001).

Record type: Article

Abstract

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 × 10^5 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.

Full text not available from this repository.

More information

Published date: November 2008
Keywords: enzyme electrode, mediator, kinetics, glucose oxidase, osmium bipyridine

Identifiers

Local EPrints ID: 145031
URI: http://eprints.soton.ac.uk/id/eprint/145031
PURE UUID: 3629970d-58c8-485e-a70f-f87c8a234f39
ORCID for P.N. Bartlett: ORCID iD orcid.org/0000-0002-7300-6900

Catalogue record

Date deposited: 15 Apr 2010 14:45
Last modified: 19 Nov 2019 02:00

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