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Sensors 2012, 12(11), 14556-14569; doi:10.3390/s121114556

Catalytic and Inhibitory Kinetic Behavior of Horseradish Peroxidase on the Electrode Surface

Department of Chemistry and State Key Laboratory of Elemento-Organic Chemistry, College of Chemistry, Nankai University, Tianjin 300071, China
Author to whom correspondence should be addressed.
Received: 2 August 2012 / Revised: 29 August 2012 / Accepted: 17 September 2012 / Published: 29 October 2012
(This article belongs to the Special Issue Enzymatic Biosensors)
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Enzymatic biosensors are often used to detect trace levels of some specific substance. An alternative methodology is applied for enzymatic assays, in which the electrocatalytic kinetic behavior of enzymes is monitored by measuring the faradaic current for a variety of substrate and inhibitor concentrations. Here we examine a steady-state and pre-steady-state reduction of H2O2 on the horseradish peroxidase electrode. The results indicate the substrate-concentration dependence of the steady-state current strictly obeys Michaelis-Menten kinetics rules; in other cases there is ambiguity, whereby he inhibitor-concentration dependence of the steady-state current has a discontinuity under moderate concentration conditions. For pre-steady-state phases, both catalysis and inhibition show an abrupt change of the output current. These anomalous phenomena are universal and there might be an underlying biochemical or electrochemical rationale. View Full-Text
Keywords: enzymatic kinetics; inhibition; anomalous behavior; electrochemical biosensor enzymatic kinetics; inhibition; anomalous behavior; electrochemical biosensor
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Huang, J.; Huang, W.; Wang, T. Catalytic and Inhibitory Kinetic Behavior of Horseradish Peroxidase on the Electrode Surface. Sensors 2012, 12, 14556-14569.

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