高等学校化学学报

高等学校化学学报 ›› 2000, Vol. 21 ›› Issue (S1): 162.

• Chemistry in Life Sciences • 上一篇    下一篇

Electrochemical Behavior from Pig Spleen Ferritin and Bacterial Ferritin of Azotobacter vinelandii

HUANG He-Qing1,2, LIN Qing-Mei2,3, WANG San-Ying1, LUO Da-Ming1   

  1. 1. School of Life Sciences, Xiamen University, Xiamen 361005;
    2. State Key Laboratory for Physical Chemistry of Solid Surfaces, Xiamen University, Xiamen 361005;
    3. Research Center of Environment Science, Xiamen University, Xiamen 361005
  • 出版日期:2000-12-31 发布日期:2000-12-31

Electrochemical Behavior from Pig Spleen Ferritin and Bacterial Ferritin of Azotobacter vinelandii

HUANG He-Qing1,2, LIN Qing-Mei2,3, WANG San-Ying1, LUO Da-Ming1   

  1. 1. School of Life Sciences, Xiamen University, Xiamen 361005;
    2. State Key Laboratory for Physical Chemistry of Solid Surfaces, Xiamen University, Xiamen 361005;
    3. Research Center of Environment Science, Xiamen University, Xiamen 361005
  • Online:2000-12-31 Published:2000-12-31

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摘要：

Being electrochemical studies, a rate of the core potential shifting to negative as a form of -205mV+(-115mV/pH) from horse spleen ferritin (HSF) has been measured by microcoulometry in the presence of mediator such as methyl viologen[1]. It was well indicated that the mediator played an important role in transferring the electrons between the ferritin and the electrode. However, using cyclic voltammetry of pulse polarography, HSF appeared appreciable currentless at the mercury electrode at scan rate 5 mV.s-1, moreover, and its mineral core isolated from protein shell showed the reductive current[2]. Evidently, these results was known that the ferritin shell be no a redox protein due to it no exhibited the current at the electrode at low potential.

Abstract:

Being electrochemical studies, a rate of the core potential shifting to negative as a form of -205mV+(-115mV/pH) from horse spleen ferritin (HSF) has been measured by microcoulometry in the presence of mediator such as methyl viologen[1]. It was well indicated that the mediator played an important role in transferring the electrons between the ferritin and the electrode. However, using cyclic voltammetry of pulse polarography, HSF appeared appreciable currentless at the mercury electrode at scan rate 5 mV.s-1, moreover, and its mineral core isolated from protein shell showed the reductive current[2]. Evidently, these results was known that the ferritin shell be no a redox protein due to it no exhibited the current at the electrode at low potential.

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