A numerical approach to modeling the catalytic voltammetry of surface-confined redox enzymes

Honeychurch, M. J. and Bernhardt, P. V. (2004) A numerical approach to modeling the catalytic voltammetry of surface-confined redox enzymes. Journal of Physical Chemistry B, 108 40: 15900-15909. doi:10.1021/jp047808g


Author Honeychurch, M. J.
Bernhardt, P. V.
Title A numerical approach to modeling the catalytic voltammetry of surface-confined redox enzymes
Journal name Journal of Physical Chemistry B   Check publisher's open access policy
ISSN 1520-6106
Publication date 2004-01-01
Sub-type Article (original research)
DOI 10.1021/jp047808g
Volume 108
Issue 40
Start page 15900
End page 15909
Total pages 10
Place of publication Washington, DC
Publisher American Chemical Society
Language eng
Subject C1
250107 Electrochemistry
780103 Chemical sciences
Abstract A finite difference method for simulating voltammograms of electrochemically driven enzyme catalysis is presented. The method enables any enzyme mechanism to be simulated. The finite difference equations can be represented as a matrix equation containing a nonlinear sparse matrix. This equation has been solved using the software package Mathematica. Our focus is on the use of cyclic voltammetry since this is the most commonly employed electrochemical method used to elucidate mechanisms. The use of cyclic voltammetry to obtain data from systems obeying Michaelis-Menten kinetics is discussed, and we then verify our observations on the Michaelis-Menten system using the finite difference simulation. Finally, we demonstrate how the method can be used to obtain mechanistic information on a real redox enzyme system, the complex bacterial molybdoenzyme xanthine dehydrogenase.
Keyword Chemistry, Physical
Mononuclear Molybdenum Enzymes
Reductive Half-reaction
Cyclic Voltammetry
Xanthine-oxidase
Adsorbed Molecules
Electron-transfer
Kinetic Control
Steady-state
Systems
Cosubstrate
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 14:04:34 EST