Mn(II)-sodium dodecyl sulphate complex mimic enzyme-catalyzed fluorescence quenching of Pyronine B by hydrogen peroxide
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Add time:09/29/2019 Source:infona.pl
Mn(II)-sodium dodecyl sulphate complex (Mn(II)-SDS) is used to mimic the active group of peroxidase. The catalytic characteristic of this mimic enzyme catalyst in the oxidation reaction of fluorescence substrate, tetraethyldiaminoxanthyl chloride (Pyronine B (PB)), with hydrogen peroxide has been studied. The experimental results show that Mn(II)-SDS complex has similar catalytic activity that of peroxidase. The steady-state catalytic rate depends upon mimic enzyme and substrate concentrations, and the Michaelis-Menten parameters K m , V m a x and K c a t are 7.6x10 - 6 M, 7.9x10 - 7 Ms - 1 and 7.9s - 1 , respectively. The catalytic activity of Mn(II)-SDS complex is compared with those of HRP and Hemin. Though the catalytic activity of Mn(II)-SDS complex is 15.9% of that of HRP, it can catalyze the oxidation reaction of PB with hydrogen peroxide lead to fluorescence quenching of PB. Under optimum conditions, linear relationship between fluorescence quenching F 0 /F and concentration of H 2 O 2 is in the range of (0.0-3.6) x 10 - 7 M. The detection limit is determined to be 3.0x10 - 9 M. By coupling this mimic catalytic reaction with the catalytic reaction of glucose oxidase (GOD), glucose can be detected. Linear relationship between F 0 /F and concentration of glucose is in the range of (0.0-1.4) x 10 - 7 M. The detection limit is determined to be 4.2x10 - 9 M. This method is applied to the determination of glucose in human serum and the results are in good agreement with the phenol-4-aminoantipyrine (4-AAP).
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