Studies on Mimic Peroxidase Behaviors of Molybdenum(VI)–Sodium Dodecyl Sulphate Complex for the Determination of Hydrogen Peroxide and Glucose

Abstract

Some transition metals–sodium dodecyl sulphate (M–SDS) complexes are used to mimic the active group of peroxidase. The catalytic characteristics of these mimic‐enzymes in the oxidation reaction of fluorescence substrate, pyronine B (PB), with hydrogen peroxide have been studied. Though the catalytic activities of M–SDS complexes are much lower than horseradish peroxidase (HRP), they can catalyze the oxidation reaction of PB with hydrogen peroxide leading to fluorescence quenching of PB. Mo(VI)–SDS complex exhibited the highest catalytic activity among same type mimic enzymes. Under optimum conditions, linear relationship between fluorescence quenching F ₀/F and concentration of H₂O₂ is in the range of 0.0–8.6 × 10⁻⁷ M. By coupling this mimic catalytic reaction with the glucose oxidase, glucose can be detected. Linear relationship between F ₀/F and concentration of glucose is in the range of 0.0–1.4 × 10⁻⁷ M. The method has been applied to the determination of glucose in human serum and the results are in good agreement with the method of phenol‐4‐aminoantipyrine.

Keywords:

• Mo(VI)–SDS complex
• Transition metals
• Mimic enzyme
• Pyronine B
• Hydrogen peroxide
• Glucose

Acknowledgment

The work is supported by the grant (No. 20075012) from National Natural Science Foundation of China.