Electron transfer reactivity and catalytic activity of structurally rigidized hemoglobin

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• 作者：Jing Wang ; Zhiqiang Liang ; Lihua Wang ; Chunhai Fan ; Genxi Li
• 关键词：Hemoglobin ; Glutaraldehyde ; Hydrogen peroxide ; Biosensor
• 刊名：Sensors and Actuators B ; Chemical
• 出版年：2007
• 期刊代码：161_09254005
• 类别：et
• 出版时间：16 July 2007
• 卷：125
• 期：1
• 页码：17-21
• 文件大小：384 K

摘要

A simple and novel strategy to obtain the direct electrochemistry of hemoglobin (Hb) was reported by enhancing its structural rigidity, which was demonstrated by the great promotion of the electron-transfer reactivity of the protein and its catalytic activity toward hydrogen peroxide (H₂O₂). Direct fast electron transfer between this structural rigidity enhanced Hb (SRE Hb) and a pyrolytic graphite (PG) electrode was achieved, and a pair of well-defined, quasi-reversible redox peaks were obtained. The cathodic and anodic peaks were located at −0.370 and −0.290 V, respectively. Meanwhile, the catalytic activity of the protein toward the reduction of H₂O₂ was also studied, and a H₂O₂ biosensor was subsequently prepared. Its detection limit was 3.4 × 10⁻⁷ M with a sensitivity of 0.0224 μA per μM of H₂O₂. The apparent Michaelis–Menten constant was calculated to be 107 μM, which was lower than those of many horseradish peroxidase based H₂O₂ sensors, suggesting that structural rigidity of Hb could endow the protein a high peroxidase activity.