Oxidation of Dibenzothiophene Catalyzed by Surfactant-Hemoprotein Complexes in Anhydrous Nonpolar Organic Solvents

  • Ryu, Keun-Garp (School of Chemical Engineering and Bioengineering, College of Engineering, The University of Ulsan) ;
  • Chae, Young-Rae (School of Chemical Engineering and Bioengineering, College of Engineering, The University of Ulsan) ;
  • Kwon, O-Yul (Department of Environmental Engineering, Seoul National University of Technology)
  • Published : 2003.10.01

Abstract

In anhydrous organic solvents, the complexes formed between AOT (dodecylbenzene sulfuric acid sodium salt) and hemoproteins, such as hemoglobin, myoglobin, or cytochrome c, displayed remarkably higher activity than the hemoprotein powders to oxidize dibenzothiophene, a model compound of organic sulfurs contained in fossil fuels. In slightly hydrophobic organic solvents, such as ethyl acetate and butyl acetate, dibenzothiophene was completely oxidized catalytically by the cytochrome c-AOT complex with cumene hydroperoxide (${\alpha},{\alpha}-dimethylbenzyl$ hydroperoxide) as an oxidant. In highly hydrophobic organic solvents, such as decane and hexadecane, however, the activity of the cytochrome c-AOT complex decreased, presumably due to the aggregation of the hemoprotein-AOT complex in these solvents.

Keywords

References

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