Studies on the interaction between cytochrome c and cis-PtCl2(NH3)2.
The interactions between cytochrome c and cis-PtCl2(NH3)2 under different conditions are reported. It is found that cis-PtCl2(NH3)2 is highly selective to bind to sulfur-containing Met residue and the interaction mode of cis-PtCl2(NH3)2 with cytochrome c is different from that of PtCl4(2-) with cytochrome c. The binding sites of platinum complex in the protein were characterized by analysis of the molar ratio of two metal atoms (Pt and Fe), 1H NMR spectra, UV-vis spectra, and differential pulse voltammetry.
Lijuan
J
J
State Key Laboratory of Coordination Chemistry, Nanjing University, People's Republic of China.
Yu
C
C
Guozi
T
T
Wenxia
T
T
D000818:Animals; D001665:Binding Sites; D002945:Cisplatin / Q000737:chemistry / Q000378:metabolism*; D003574:Cytochrome c Group / Q000737:chemistry / Q000378:metabolism*; D066298:In Vitro Techniques; D007501:Iron / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010984:Platinum / Q000737:chemistry
D003574:Cytochrome c Group; D010984:Platinum; D007501:Iron; D002945:Cisplatin