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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 Fe 3+/Fe 2+(E m7) 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.
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 of reversed micelle acts as a certain orientation surrounding medium, it offers a strong electrostatic field that alters the reductive potential of Fe 3 + / Fe 2+ (E m7) in the heme of hemeproteins and then the the catalytic activity of peroxidase accordingly. According to the results of UV-Vis, 1H NMR and FTIR, the polymer catalyzed by hemoglobin (Hb) in presumed to be constructed of lines and trapeziforms alternatively.