Peculiar Features in the Crystal Structure of the Adduct Formed between cis-PtI2(NH3)2 and Hen Egg White Lysozyme
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文摘
The reactivity of cis-diamminediiodidoplatinum(II), cis-PtI2(NH3)2, the iodo analogue of cisplatin, with hen egg white lysozyme (HEWL) was investigated by electrospray ionization mass spectrometry and X-ray crystallography. Interestingly, the study compound forms a stable 1:1 protein adduct for which the crystal structure was solved at 1.99 脜 resolution. In this adduct, the PtII center, upon release of one ammonia ligand, selectively coordinates to the imidazole of His15. Both iodide ligands remain bound to platinum, with this being a highly peculiar and unexpected feature. Notably, two equivalent modes of PtII binding are possible that differ only in the location of I atoms with respect to ND1 of His15. The structure of the adduct was compared with that of HEWL鈥揷isplatin, previously described; differences are stressed and their important mechanistic implications discussed.
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