Catalytic aerobic oxidation of 2-chloroethyl ethylsulfide, a mustard simulant, under ambient conditions - Effect of solvents, ligands, and transitionmetals on reactivity

The complexes Au(III)(Hal)(2)(NOx)(L), Hal = Cl- or Br-, NOx = NO3- or NO2- , L = thioether, catalyze the selective aerobic sulfoxidation of thioethers , including the mustard simulant 2-chloroethyl ethyl sulfide (CEES), by dio xygen (stoichiometry: CEES + 0-5O(2) --> CEESO) under ambient conditions (2 5 degreesC, I atm O-2) in both homogeneous solution (acetonitrile, trifluor oethanol, nitromethane, 1,2-dichloroethane) or non-toxic perfluoropolyether (PFPE) suspensions. The reaction rate, induction period, and the extent of product inhibition are dependent on the Au(III) ligands, the solvent, and the presence of additional redox active metals. Catalytic aerobic CEES oxid ation is 1.8 times faster when NO3- is replaced by NO2- and 3.3 times faste r when Cl- is replaced by Br- in acetonitrile. This reaction in trifluoroet hanol exhibits no induction period and is 2.8 times faster than in acetonit rile. Addition of 2 equiv. of Cu(II) per Au(Ill) to the system increases th e rate by a factor of 2.7. The Au(III)/(Br-)(2)/NO3-/Cu(II) system exhibits high rates for the selective aerobic oxidation of CEES to CEESO under ambi ent conditions (similar to 68 turnovers per hour), with little if any inhib ition by the CEESO product. At low concentrations, sulfoxides reduce the in duction period and increase the rate of CEES oxidation in acetonitrile, but at high concentrations they inhibit the reaction. These Au(Ill) catalysts are extremely efficient for aerobic CEES sulfoxidation when suspended in th e PFPE Fomblin (R) MF-300 (up to 200 turnovers in 10 min). This is a signif icant improvement from the Au system described in the first study, Au(III)( Cl)(2)(NO3)(CEES) in acetonitrile, which yielded approximately 5 turnovers of CEESO after 10 min. The catalytic reactivity of the Au(III)(Cl)(2)(NO3)( L) in Fomblin (R) MF-300 for aerobic CEES oxidation was evaluated in the pr esence of the common amino acids to assess the extent to which the various functional groups in human skin (epidermal polypeptides) might inhibit the catalysis. Some amino acids inhibit the reaction, but the reaction still pr oceeds even in the presence of 7.5 equiv. of the most inhibitory functional group, indole (tryptophan). (C) 2001 Elsevier Science B.V. All rights rese rved.