[Research on the mechanism of fluorescence quenching of HRP by NaN3].
The fluorescence and synchronous fluorescence spectra were employed to study the binding between sodium azide (NaN3) and horseradish peroxidase (HRP), which was affected by the molecular conformation and the microenvironment of the fluorescence residues. The mechanism of the fluorescence quenching of HRP by NaN3 was discussed and the binding constant and the number of binding sites of non-covalent bond between them were calculated.
Xia
Bing-le
BL
University of Science and Technology of China, Chemistry Department, Hefei 230026, China.
Peng
Dun-geng
DG
Niu
Hai-xia
HX
Liu
Qing-liang
QL
D000465:Algorithms; D001665:Binding Sites; D005453:Fluorescence; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D011485:Protein Binding; D012107:Research Design; D019810:Sodium Azide / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods*
D019810:Sodium Azide; D006735:Horseradish Peroxidase