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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; in revised form: 29 August 2012 / Accepted: 17 September 2012 / Published: 29 October 2012
Abstract: 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.
Keywords: enzymatic kinetics; inhibition; anomalous behavior; electrochemical biosensor
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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.
Huang J, Huang W, Wang T. Catalytic and Inhibitory Kinetic Behavior of Horseradish Peroxidase on the Electrode Surface. Sensors. 2012; 12(11):14556-14569.
Huang, Jitao; Huang, Wei; Wang, Titi. 2012. "Catalytic and Inhibitory Kinetic Behavior of Horseradish Peroxidase on the Electrode Surface." Sensors 12, no. 11: 14556-14569.