摘要

Efforts to replace native peroxidase with its low molecular weight alternatives have stimulated a search for peroxidase mimetics. Herein we describe the oxidation of luminol with hydrogen peroxide catalyzed by commercially available Fe-III-TAML activator 1a, which was shown to be a more active catalyst than hemin. At Fe-III-TAML activator 1a use in chemiluminescent assay for H2O2 determination the detection limit value (3 sigma) of 5 x 10(-8) M was similar to the detection limit obtained with horseradish peroxidase (1 x 10(-7) M) and significantly lower than that obtained in the presence of hemin (6 x 10(-7) M). The linear ranges (R-2=0.98) of the assay were 6 x 10(-8)-1 x 10(-6) M and 6 x 10(-7)-1 x 10(-6) M H2O2 for Fe-III-TAML la and hemin, respectively. The CV values for Fe-III-TAML la-based assay measured within the working range varied from 1.0% to 3.7% (n=4), whereas in the case of hemin -5.0% to 9.7% (n=4). Moreover, the sensitivity of Fe-III-TAML 1a-based method was 56 and 5 times higher than that of hemin-and HRP-based methods, respectively. The obtained results open good perspectives to apply Fe-III-TAML activator 1a in CL analytical methods instead of hemin, a traditionally used peroxidase mimetic.

  • 出版日期2014-7-1