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Tessier, Christian; Rochon, Fernande D; Beauchamp, André L
Inorganic chemistry, 11/2004, Letnik: 43, Številka: 23Journal Article
The ReOX2(met) compounds (X = Cl, Br) adopt a distorted octahedral structure in which a carboxylato oxygen lies trans to the ReO bond, whereas the equatorial plane is occupied by two cis halides, an NH2, and an SCH3 group. Coordination of the SCH3 unit creates an asymmetric center, leading to two diastereoisomers. X-ray diffraction studies reveal that the crystals of ReOBr2(d,l-met)·1/2H2O and ReOBr2(d,l-met)·1/2CH3OH contain only the syn isomer (S−CH3 bond on the side of the ReO bond), whereas ReOCl2(d-met) and ReOCl2(d,l-met) consist of the pure anti isomer. 1H NMR spectroscopy shows that both isomers coexist in equilibrium in acetone (anti/syn ratio = 1:1 for X = Br, 3:1 for X = Cl). Exchange between these two isomers is fast above room temperature, but it slows down below 0 °C, and the sharp second-order spectra of both isomers at −20 °C were fully assigned. The coupling constants are consistent with the solid-state conformations being retained in solution. Complexes of the type ReOX2(His-aa)X (X = Cl, Br) are isolated with the dipeptides His-aa (aa = Gly, Ala, Leu, and Phe). X-ray diffraction work on ReOBr2(His-Ala)Br reveals the presence of distorted octahedral cations containing the ReO3+ core and a dipeptide coordinated through the histidine residue via the imidazole nitrogen, the terminal amino group, and the amide oxygen, the site trans to the ReO bond being occupied by the oxygen. The alanine residue is ended by a protonated carboxylic group that does not participate in the coordination. The constant pattern of the1H NMR signals for the protons in the histidine residue confirms that the various dipeptides adopt a similar binding mode, consistent with the solid-state structure being retained in CD3OD solution.
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