CRCU

Chemical Research in Chinese Universities ›› 2004, Vol. 20 ›› Issue (2): 240-243.

• Articles • Previous Articles     Next Articles

Polymerization of o-Phenylenediamine Catalyzed by Hemeproteins Encapsulated in Reversed Micelle

YANG Yong, MAO Lu-yuan, LI Liu-zhu, LIU Xiao-guang, SHI Jun, CAO Shao-kui   

  1. Lab of Biomimetic Macromolecule, College of Materials Engineering, Zhengzhou University, Zhengzhou 450052, P. R. China
  • Received:2003-12-05 Online:2004-04-24 Published:2011-08-06
  • Supported by:

    Supported by the Natural Science Fund of Henan Province (No.20024300006)and by the Natural Science Fund of Henan Province High Education of China(No.0211021000).

PDF (PC)

Cited

23

Abstract: Hemeproteins encapsulated in reversed micelle formulated with di-2-ethylhexyl sulfosuccinate (AOT)was found to catalyze the polymerization of o-phenylenediamine (o-PDA) with hydrogen peroxide, whereas o-PDA catalyzed by hemeproteins dissolved in water could only form its trimers. As the nanostructural environment in reversed micelle acts as a certain orientation surrounding medium, it offers a strong electrostatic field that alters the reductive potential of Fe3+/Fe2+ (Em7) in the heme of hemeproteins and thus increases the catalytic activity of peroxidase accordingly. According to the results of UV-Vis, 1H NMR and FTIR, the polymer catalyzed by hemoglobin(Hb) in reversed micelle was presumed to be constructed of lines and trapeziforms alternatively.

Key words: Hemeprotein, Hemoglobin, Horseradish peroxidase, Reversed micell, o-Phenylenediamine