| 19267501 |
Bhabak KP, Mugesh G: A synthetic model for the inhibition of glutathione peroxidase by antiarthritic gold compounds. Inorg Chem. 2009 Mar 16;48(6):2449-55.
In this paper, inhibition of the glutathione peroxidase activity of two synthetic organoselenium compounds, bis [2-(N,N-dimethylamino) benzyl] diselenide (5) and bis [2-(N,N-dimethylamino) benzyl] selenide (9), by gold (I) thioglucose (1), chloro (triethylphosphine) gold (I), chloro (trimethylphosphine) gold (I), and chloro (triphenylphosphine) gold (I) is described. The inhibition is found to be competitive with respect to a peroxide (H (2) O (2)) substrate and noncompetitive with respect to a thiol (PhSH) cosubstrate. The diselenide 5 reacts with PhSH to produce the corresponding selenol (6), which upon treatment with 1 equiv of gold (I) chlorides produces the corresponding gold selenolate complexes 11-13. However, the addition of 1 equiv of selenol 6 to complexes 11-13 leads to the formation of bis-selenolate complex 14 by ligand displacement reactions involving the elimination of phosphine ligands. The phosphine ligands eliminated from these reactions are further converted to the corresponding phosphine oxides (R (3) PO) and selenides (R (3) PSe). In addition to the replacement of the phosphine ligand by selenol 6, an interchange between two different phosphine ligands is also observed. For example, the reaction of complex 11 having a trimethylphosphine ligand with triphenylphosphine produces complex 13 by phosphine interchange reactions via the formation of intermediates 15 and 16. The reactivity of selenol 6 toward gold (I) phosphines is found to be similar to that of selenocysteine. |
31(0,1,1,1) |