Ferraro Giarita, Massai Lara, Messori Luigi, Cinellu Maria Agostina, Merlino Antonello
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, 80126, Naples, Italy.
Biometals. 2015 Aug;28(4):745-54. doi: 10.1007/s10534-015-9863-7. Epub 2015 Jun 9.
A new crystal structure is reported here for the adduct formed in the reaction between NH4 [Au(Sac)2], AuSac2, a cytotoxic homoleptic gold(I) complex with the saccharinate ligand, and the model protein hen egg white lysozyme. To produce this adduct, AuSac2 breaks down and releases both saccharinate ligands. The resulting Au(I) ions bind the protein to ND1 and NE2 atoms of His15 but also to SD atom of the zero-solvent accessible Met105 side chain, which is located in the protein hydrophobic box. The unexpected existence of this secondary gold(I) binding site is confirmed by spectroscopic and spectrometric measurements in solution.
本文报道了一种新的晶体结构，该结构是由NH4[Au(Sac)2]（AuSac2，一种具有糖精配体的细胞毒性同配金（I）配合物）与模型蛋白鸡蛋清溶菌酶反应形成的加合物。为了产生这种加合物，AuSac2分解并释放出两个糖精配体。生成的Au（I）离子与蛋白质结合到His15的ND1和NE2原子上，同时也与位于蛋白质疏水盒中的零溶剂可及的Met105侧链的SD原子结合。溶液中的光谱和光谱测量证实了这个二级金（I）结合位点的意外存在。
