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Direct electrochemistry and electrocatalysis of hemoglobin at three-dimensional gold film electrode modified with self-assembled monolayers of 3-mercaptopropylphosphonic acid

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Title: Direct electrochemistry and electrocatalysis of hemoglobin at three-dimensional gold film electrode modified with self-assembled monolayers of 3-mercaptopropylphosphonic acid
Authors: Chen, Yu1, Yang, Xiao-Jing1, Guo, Li-Rong1, Li, Jing2, Xia, Xing-Hua2 xhxia@nju.edu.cn, Zheng, Li-Min1 lmzheng@nju.edu.cn
Source: Analytica Chimica Acta. Jun2009, Vol. 644 Issue 1/2, p83-89. 7p.
Subjects: Electrocatalysis, Electrochemistry, Hemoglobins, Gold compounds, Metallic films, Electrodes, Molecular self-assembly, Phosphonic acids
Abstract: Abstract: Multilayered hemoglobin (Hb) molecules were successfully immobilized on three-dimensional gold film electrode modified with self-assembled monolayers (SAMs) of 3-mercaptopropylphosphonic acid. Direct electrochemistry of the immobilized multilayered Hb occurs with high thermal stability and electrochemical stability. In the multilayered Hb film, the most inner Hb molecules can directly transfer electron with the electrode, while the Hb protein beyond this layer communicates electron with the electrode via protein–protein electron exchange. In addition, the proposed functional interface can greatly enhance electron transfer rate of the immobilized Hb protein (k s =15.8±2.0s−1) due to the increase of roughness of the gold substrate. Under optimized experimental conditions, the multilayered Hb film displays good bioelectrocatalytic activity toward the reduction of hydrogen peroxide. This electrochemical sensor shows fast response (less than 1s), wide linear range (7.8×10−8 to 9.1×10−5 M) and low detection limit (2.5×10−8 M), which can be attributed to good mass transport, large Hb proteins loading per unit area and fast electron transfer rate of Hb protein. [Copyright &y& Elsevier]
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Database: Engineering Source
Description
Abstract:Abstract: Multilayered hemoglobin (Hb) molecules were successfully immobilized on three-dimensional gold film electrode modified with self-assembled monolayers (SAMs) of 3-mercaptopropylphosphonic acid. Direct electrochemistry of the immobilized multilayered Hb occurs with high thermal stability and electrochemical stability. In the multilayered Hb film, the most inner Hb molecules can directly transfer electron with the electrode, while the Hb protein beyond this layer communicates electron with the electrode via protein–protein electron exchange. In addition, the proposed functional interface can greatly enhance electron transfer rate of the immobilized Hb protein (k s =15.8±2.0s−1) due to the increase of roughness of the gold substrate. Under optimized experimental conditions, the multilayered Hb film displays good bioelectrocatalytic activity toward the reduction of hydrogen peroxide. This electrochemical sensor shows fast response (less than 1s), wide linear range (7.8×10−8 to 9.1×10−5 M) and low detection limit (2.5×10−8 M), which can be attributed to good mass transport, large Hb proteins loading per unit area and fast electron transfer rate of Hb protein. [Copyright &y& Elsevier]
ISSN:00032670
DOI:10.1016/j.aca.2009.04.027