Abstract
The unique capacity of the Mo24+ cation to form complexes with polypeptide ligands in which only the carboxyl terminus is coordinated and the rest of the zwitterionic molecule is left conformationally free is described. This principle is then illustrated by the isolation and structural characterization of the [Mo2(glycylglycine)4]4+ ion in the form of the compound [Mo2(GG)4]Cl4'6H20. The structure has been solved and refined in space group l with Z= 1 by conventional methods using diffractometer data. The unit cell dimensions are a = 9.775 (2) A. 6 = 10.886 (2) Á,c = 9.495 (2) Á, a = 107.06 (2)°, ß = 113.15 (2)°, 7 = 91.07 (2)°, V = 877.8 (1) A3. Each of the two crystallographically independent glycylglycine ligands contains a central peptide linkage that conforms very closely to the generally accepted standard dimensions and planar trans conformation for peptide links.
Original language | English |
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Pages (from-to) | 3014-3017 |
Number of pages | 4 |
Journal | Journal of the American Chemical Society |
Volume | 102 |
Issue number | 9 |
DOIs | |
State | Published - Apr 1980 |
Externally published | Yes |