• Title/Summary/Keyword: Light-Induced Mitochondrial $F_0F_1-ATPase$

Search Result 2, Processing Time 0.014 seconds

Study on the Light-Induced Mitochondrial ATPase$(F_1-ATPase)$ Activated by Iron ion in Mushroom (버섯중 철이온에 활성화된 광감응성 Mitochondrial ATPase에 관한 연구)

  • Min, Tae-Jin;Lee, Mi-Ae;Park, Sang-Shin
    • The Korean Journal of Mycology
    • /
    • v.21 no.3
    • /
    • pp.157-164
    • /
    • 1993
  • The effects of the iron ions on the light-induced mitochondrial $F_1-ATPase$ in Lentinus edodes was studied. This enzyme activity was stimulated by each of the ferric, ferrous and magnesium ion. Especially, the activity of the enzyme by 5.0 mM ferric ion increased up to 107% in comparision with control group(100%). In the presence of magnesium ion, each of ferric and ferrous ion increased the activity of the enzyme, particulary, coexistence of 0.1 mM magnesium and 5.0 mM ferric ion increased the activity up to 270% with magnesium ion dependence. The activity of the enzyme was stimulated up to 268% by 5.0 mM ferric ion in the presence of 0.1 mM magnesium and 0.1 mM ferrous ion. Therefore, the coexistence of ferrous ion did not affect the activity. From the above, we propose that light-induced mitochondrial $F_1-ATPase$ in Lentinus edodes is a $Mg^{2+}{\cdot}Fe^{3+}{\;}F_1-ATPase.$ The optimal pH and temperature for the enzyme were 7.5 and $66^{\circ}C$ respectively.

  • PDF

Study on the Enzyme of Basidiomycetes(I) -The Effects of Iron Ions on the Light-Induced Mitochondrial $F_0F_1-ATPase$ of Lentinus edodes- (담자균류의 효소에 관한 연구(I) -표고버섯 중의 광감응성 Mitochondrial $F_0F_1-ATPase$의 철이온 효과-)

  • Min, Tae-jin;Lee, Mi-Ae;Bae, Kang-Gyu
    • The Korean Journal of Mycology
    • /
    • v.21 no.3
    • /
    • pp.165-171
    • /
    • 1993
  • The effects of the iron ions for the light-induced mitochondrial $F_0F_1-ATPase$ of Lentinus edodes was studied. The enzyme activity was stimulated up to 202% by 0.1 mM $Fe^{2-}$ ion, but was inhibited by $Fe^{3+}\;and\;Mg^{2+}$. In the presence of 0.5 mM $Mg^{2+}$, the activity also increased 32% by 0.1 mM $Fe^{2+}$ ion, and decreased to a similar extent by $Fe^{3+}$ ion than by only $Fe^{3+}$ ion. Also, the activity was inhibited 53% by 5.0 mM $Fe^{2-}$ ion in the presence of 0.5 mM $Mg^{2+}$ ion and various concentration of $Fe^{3+}$ ion(mM). These results showed that $Fe^{2+}$ strongly stimulated the enzyme activity and its role for the enzyme was independent of $Mg^{2+}$ ion, but was dependent of $Fe^{3+}$ ion. From inactivation of the enzyme by addition of metal chelating agent, EDTA, it is suggested that the enzyme is to be metalloenzyme. The optimal pH and temperature of the enzyme in the presence of 0.1 mM $Fe^{2+}$ was 7.6 and $63^{\circ}C$, respectively.

  • PDF