Premium
Studies on the interaction of palmatine hydrochloride with bovine hemoglobin
Author(s) -
Liu Baosheng,
Yan Xiaona,
Cao Shina,
Chong Baohong,
Lü Yunkai
Publication year - 2014
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2529
Subject(s) - chemistry , circular dichroism , palmatine , quenching (fluorescence) , hydrochloride , metal ions in aqueous solution , hemoglobin , tryptophan , metal , crystallography , stereochemistry , analytical chemistry (journal) , chromatography , organic chemistry , fluorescence , amino acid , alkaloid , biochemistry , physics , quantum mechanics
The interaction between bovine hemoglobin (BHb) and palmatine hydrochloride (PMT) was investigated at different temperatures using multispectroscopy, as well as the effect of common metal ions (Ca 2+ , Mg 2+ , Zn 2+ , Cu 2+ , Fe 2+ , Fe 3+ , Co 2+ , Ni 2+ ) on the BHb–PMT system. Results showed that the quenching mechanism of PMT on BHb was a static process. The electrostatic force played an important role in the conjugation reaction between BHb and PMT. The order of magnitude of the binding constants ( K a ) was 10 4 , and the number of binding sites ( n ) in the binary system was ~ 1. The binding distance ( r ) was ~ 2.44 nm and the primary binding for PMT was located at β‐37 tryptophan in the hydrophobic cavity of BHb. In addition, the Hill's coefficients were ~ 1. Synchronous and circular dichroism spectra revealed that the microenvironment and the conformation of BHb were changed during the binding reaction. Copyright © 2013 John Wiley & Sons, Ltd.