A Numerical Approach to Modeling the Catalytic Voltammetry of Surface-Confined Redox Enzymes
Autor: | Michael J. Honeychurch, Paul V. Bernhardt |
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Rok vydání: | 2004 |
Předmět: |
Steady state
Chemistry Quantitative Biology::Molecular Networks Inorganic chemistry Finite difference method Surfaces Coatings and Films Enzyme catalysis Quantitative Biology::Subcellular Processes Nonlinear system Electron transfer Materials Chemistry Physical and Theoretical Chemistry Cyclic voltammetry Biological system Voltammetry Sparse matrix |
Zdroj: | The Journal of Physical Chemistry B. 108:15900-15909 |
ISSN: | 1520-5207 1520-6106 |
DOI: | 10.1021/jp047808g |
Popis: | 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. |
Databáze: | OpenAIRE |
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