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Citation: Dai Zhi-Hui, Ju Huang-Xian. Direct Electron Transfer of Protein Immobilized on Mesoporous Molecular Sieves Matrix[J]. Acta Physico-Chimica Sinica, ;2004, 20(10): 1262-1266. doi: 10.3866/PKU.WHXB20041020 shu

Direct Electron Transfer of Protein Immobilized on Mesoporous Molecular Sieves Matrix

1.
Department of Chemistry, Key Laboratory of Analytical Chemistry for Life Science, Ministry of Education of China, Nanjing University, Nanjing　210093

Received Date: 2 April 2004
Available Online: 15 October 2004

The direct electron transfer of different heme proteins immobilized on mesoporous molecular sieves was studied. The direct electrochemistry of horseradish peroxidase (HRP), hemoglobin (Hb) and myoglobin (Mb) immobilized on hexa nal mesoporous silica (HMS) was described, respectively. The immobilized heme proteins at modified glassy carbon electrodes (GCE) showed od direct electrochemical behaviors, which depended on the specific properties of the HMS. Two couples of redox peaks corresponding to the Fe(III) to Fe(II) conversion of the proteins intercalated in the mesopores and adsorbed on the surface of the HMS in 0.1 mol•L－1, pH 7.0 PBS (phosphate-buffered saline), respectively, were observed. The amount of proteins intercalated in the mesopores of HMS was proved to be related to the porous size. The result showed the electrode processes to be surface-controlled electrode processes with a single proton transfer. The interactions between proteins and HMS were investigated by using FT-IR, N2 adsorption isotherms and electrochemical methods, and the new biosensors of hydrogen peroxide (H2O2) and nitrite (NO2－) were constructed. These works extended the application of HMS in immobilizing protein, the direct electron transfer of protein and the construction of reagentless biosensors.
- Proteins;Mesoporous molecular sieves;Direct electrochemistry;　Interaction;Biosensors
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