Experimental and theoretical studies on inversion dynamics of dichloro(L-difluoromemionine-N,S)platinum(II) and dichloro(L-trifluoromethionine-N,S)platinum(II) complexes

摘要

Fluorinated analogues of methionine such as L-S-(difluoromethyl)homocysteine (L-difluoromethionine;DFM) and L-S-(trifluoromethyl)ho-mocysteine (L-trifluoromethionine;TFM) have been demonstrated to be interesting analogues for incorporation into peptides and proteins.The presence of the fluorine nucleus adjacent to the sulfur atom in the side chain not only serves to alter the nucleophilicity and electron density of the sulfur atom but it can function as an important NMR spectroscopic (~(19)F) probe.Additional information on the properties of these fluorinated amino acid analogues was obtained by studying their interactions with dipotassium tetrachloroplatinate (K_2PtCl_4).The resulting complexes,dichloro(L-difluoromethionine-N,S)platinum(II) and dichloro(L-trifluoromethionine-N,S)platinum(II) were investigated with respect to their sulfur inversion rates utilizing dynamic NMR methods.Inversion barriers for the DFM-and TFM-platinum complexes were experimentally determined to be 16.4+-0.2 and 18+-1 kcal/mol,respectively.Density functional calculations at the B3LYP/SDD level were also performed to model the structures and energies of the ground and transition states for these complexes.