Binding of Al(III)-tetracarboxyphthalocyanine to hemoglobin and myoglobin.
The interactions between Al(III)-tetracarboxyphthalocyanine (AlPc(COOH)(4)) and hemoglobin (or myoglobin) have been studied. The results showed that AlPc(COOH)(4) effectively quenched the intrinsic fluorescence of Hb and Mb via static quenching. The hydrophobic and electrostatic interactions played a major role in stabilizing the AlPc(COOH)(4)-protein complex. The distance r between donor and acceptor was obtained to be 3.92 and 3.67 nm for AlPc(COOH)(4)-Hb and AlPc(COOH)(4)-Mb system, respectively. The effect of AlPc(COOH)(4) on the conformation of Hb and Mb was analyzed using UV-vis absorption spectroscopy, circular dichroism spectra, synchronous fluorescence and three-dimensional fluorescence spectra.
Zhou
Qiu-Hua
QH
Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng, China.
Zhang
Hong-Mei
HM
Wu
Lin
L
Wang
Yan-Qing
YQ
D000535:Aluminum / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D006736:Horses; D006801:Humans; D007211:Indoles / Q000737:chemistry / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism*; D009942:Organometallic Compounds / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics
D006454:Hemoglobins; D007211:Indoles; D009211:Myoglobin; D009942:Organometallic Compounds; D000535:Aluminum