Electron transfer reactivity and the catalytic activity of horseradish peroxidase incorporated in dipalmitoylphosphatidic acid films.
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.
Department of Biochemistry and National Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, PR China.
Xinjian
X
Liu
Yinxi
Y
Huang
Libin
L
Shang
Xiaoyue
X
Wang
Han
H
Xiao
Genxi
G
Li
D002384:Catalysis; D004566:Electrodes; D004579:Electron Transport; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D015394:Molecular Structure; D010100:Oxygen / Q000737:chemistry; D010712:Phosphatidic Acids / Q000737:chemistry*; D013053:Spectrophotometry
D010712:Phosphatidic Acids; C031599:dipalmitoylphosphatidic acid; D006735:Horseradish Peroxidase; D010100:Oxygen