Title of article :
Studies on direct electron transfer and biocatalytic properties of heme proteins in lecithin film Original Research Article
Author/Authors :
Qing Lu، نويسنده , , Xiaoxia Chen، نويسنده , , Yunhua Wu، نويسنده , , Shengshui Hu، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Pages :
9
From page :
55
To page :
63
Abstract :
Myoglobin (Mb), hemoglobin (Hb) and horseradish peroxidase (HRP) were incorporated in lecithin (PC) film on glassy carbon (GC) electrode by the method of vesicle-fusion. A pair of well-defined and quasi-reversible cyclic voltammetric peaks was obtained, which reflected the direct electron transfer of heme proteins. UV–Vis and reflectance absorption infrared (RAIR) spectroscopy showed that proteins in PC films remained at their secondary structure similar to their native states. Scanning electron microscopy (SEM) demonstrated the interaction between the proteins and PC would make the morphology of protein-PC films very different from the PC films alone. The immobilized proteins retained their biocatalytic activity to the reduction of NO and hydrogen peroxide, which provide the perspective to be the third generation sensors.
Keywords :
Myoglobin , Hemoglobin , Horseradish peroxidase , Direct electron transfer , Lecithin
Journal title :
Biophysical Chemistry
Serial Year :
2005
Journal title :
Biophysical Chemistry
Record number :
1113710
Link To Document :
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