کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1952241 1057198 2010 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Iron transport by proteoliposomes containing mitochondrial F1Fo ATP synthase isolated from rat heart
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Iron transport by proteoliposomes containing mitochondrial F1Fo ATP synthase isolated from rat heart
چکیده انگلیسی

In this work, we present evidence of Fe2+ transport by rat heart mitochondrial F1Fo ATP synthase. Iron uptake by the vesicles containing the enzyme was concentration- and temperature-dependent, with an optimum temperature of 37 °C. Both ATP and ADP stimulated iron uptake in a concentration-dependent manner, whereas AMP, AMPPCP, and mADP did not. Inhibitors of the enzyme, oligomycin, and resveratrol similarly blocked iron transport. The iron uptake was confirmed by inhibition using specific antibodies against the α, β, and c subunits of the enzyme. Interestingly, slight transport of common divalent and trivalent metal ions such as Mg+2, Ca+2, Mn+2, Zn+2, Cu+2, Fe+3, and Al+3 was observed. Moreover, Cu+2, even in the nM range, inhibited iron uptake and attained maximum inhibition of approximately 56%. Inorganic phosphate (Pi) in the medium exerted an opposite effect depending on the type of adenosine nucleotide, which was suppressed with ATP, but enhanced with ADP. A similarly stimulating effect of ATP and ADP with an inverse effect of Pi suggests that the activity of ATPase and ATP synthase may be associated with iron uptake in a different manner, probably via antiport of H+.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 92, Issue 4, April 2010, Pages 333–342
نویسندگان
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