[Study on the mechanism of interaction between TH-PF-Mo(VI) complex and bovine serum albumin by fluorimetric method].
The mechanism of interaction between bovine serum albumin (BSA) and trihydroxylphenylfluorone (TH-PF)-Mo(VI) complex in neutral solution was studied by fluorimetric method. The mechanism of fluorescence quenching of BSA caused by (TH-PF)-Mo(VI) complex probe was investigated and the binding constants under different temperature were measured. The binding constants of the reaction at 25 degrees C and 40 degrees C were calculated by fluorimetric method to be 4.78 x 10(4) L x mol(-1) and 3.72 x 10(4) L x mol(-1), respectively. According to the theory of Forster non-radiation energy transfer, the binding distance and transfer efficiency at 25 degrees C were calculated to be 2.89 nm and 0.314, respectively. Furthermore, the thermodynamic parameters were measured and the results indicated that electrostatic force played a major role in the interaction between TH-PF-Mo(VI) complex and BSA.
Huang
Jian-hua
JH
Department of Chemical Engineering, Henan Institute of Science and Technology, Xinxiang 453003, China.
Ma
Hong-min
HM
Sun
Shu-ting
ST
Chen
Xin
X
Dong
Hai-xia
HX
Wei
Qin
Q
D000818:Animals; D002417:Cattle; D005452:Fluoresceins / Q000737:chemistry*; D005470:Fluorometry; D008982:Molybdenum / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*
D005452:Fluoresceins; D012710:Serum Albumin, Bovine; C010159:fluorone Black; D008982:Molybdenum