高等学校化学学报 ›› 2000, Vol. 21 ›› Issue (S1): 183.

• Chemistry in Life Sciences • 上一篇    下一篇

The Electrode Behavior and the Storing Capacity from Liver Ferritin of Dasynatis Akajei

HUANG He-Qing1,2, LIN Qing-Mei3, KONG Bo1   

  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

The Electrode Behavior and the Storing Capacity from Liver Ferritin of Dasynatis Akajei

HUANG He-Qing1,2, LIN Qing-Mei3, KONG Bo1   

  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

摘要:

Ferritin, a metallic protein, is a special biological large molecule that plays two central physiological functions in living cell simultaneously[1]. In addition, the ferritin is able to express two functions having activity of H2-uptake and exhibiting electrode behavior that picks the electrons up from a bare platinum electrode directly under anaerobic condition[2-3]. In this paper, a direct electrochemical technology under aerobic conditions is employed to study kinetics of iron release from liver ferritin of Dasyatis akajei (DALF). Using aerobic condition, an electron tunnel across the ferritin shell plays still a critical role in taking the electrons from a bare platinum electrode for iron release without any mediator aid. Moreover, using similar condition, two reduction potentials of the ferritin core with -135 mV and -416 mV vs. NHE are measured by the technology. Unlike other processes of iron release, a kinetic study for complete iron release is confirmed to show a triphasic behavior defined as zero-order reaction. DALF is known to heme bind to generate a hemeoprotein, named DALFh The heme function has been investigated to accelerate rate of iron release. Using similar studies, the kinetic datum indicates that the rate of iron release depends tightly on not only the reduction potential of the electrode, but also the regulation capacity of protein shell itself.

Abstract:

Ferritin, a metallic protein, is a special biological large molecule that plays two central physiological functions in living cell simultaneously[1]. In addition, the ferritin is able to express two functions having activity of H2-uptake and exhibiting electrode behavior that picks the electrons up from a bare platinum electrode directly under anaerobic condition[2-3]. In this paper, a direct electrochemical technology under aerobic conditions is employed to study kinetics of iron release from liver ferritin of Dasyatis akajei (DALF). Using aerobic condition, an electron tunnel across the ferritin shell plays still a critical role in taking the electrons from a bare platinum electrode for iron release without any mediator aid. Moreover, using similar condition, two reduction potentials of the ferritin core with -135 mV and -416 mV vs. NHE are measured by the technology. Unlike other processes of iron release, a kinetic study for complete iron release is confirmed to show a triphasic behavior defined as zero-order reaction. DALF is known to heme bind to generate a hemeoprotein, named DALFh The heme function has been investigated to accelerate rate of iron release. Using similar studies, the kinetic datum indicates that the rate of iron release depends tightly on not only the reduction potential of the electrode, but also the regulation capacity of protein shell itself.

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