Journal
BIOELECTROCHEMISTRY
Volume 68, Issue 1, Pages 98-104Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2005.05.004
Keywords
horseradish peroxidase; dipalmitoylphosphatidic acid; hydrogen peroxide; nitric oxide; cyclic voltammetry
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Horseradish peroxidase (HRP) was incorporated in dipalmitoylphosphatidic acid (DPPA) to form a film and the film was modified on pyrolytic graphite electrode. UV-Vis spectra suggested that HRP in the film could keep its secondary structure similar to the native state. A pair of stable, well-defined, and quasi-reversible cyclic voltammetric peaks was observed with the formal potential at -276.2 mV (vs. saturated calomel electrode), characteristic of heme Fe-III/Fe-II redox couple of HRP. The apparent heterogeneous electron transfer rate constant and other electrochemical parameters were presented. The catalytic activity of HRP in DPPA film toward oxygen, hydrogen peroxide and nitric oxide were also examined. (c) 2005 Elsevier B.V. All rights reserved.
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