کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5507123 | 1537039 | 2017 | 22 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural and kinetics characterization of the F1F0-ATP synthase dimer. New repercussion of monomer-monomer contact
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
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چکیده انگلیسی
Ustilago maydis is an aerobic basidiomycete that fully depends on oxidative phosphorylation for its supply of ATP, pointing to mitochondria as a key player in the energy metabolism of this organism. Mitochondrial F1F0-ATP synthase occurs in supramolecular structures. In this work, we isolated the monomer (640Â kDa) and the dimer (1280Â kDa) and characterized their subunit composition and kinetics of ATP hydrolysis. Mass spectrometry revealed that dimerizing subunits e and g were present in the dimer but not in the monomer. Analysis of the ATPase activity showed that both oligomers had Michaelis-Menten kinetics, but the dimer was 7 times more active than the monomer, while affinities were similar. The dimer was more sensitive to oligomycin inhibition, with a Ki of 24Â nM, while the monomer had a Ki of 169Â nM. The results suggest that the interphase between the monomers in the dimer state affects the catalytic efficiency of the enzyme and its sensitivity to inhibitors.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1858, Issue 12, December 2017, Pages 975-981
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1858, Issue 12, December 2017, Pages 975-981
نویسندگان
Mercedes Esparza-PerusquÃa, SofÃa Olvera-Sánchez, Juan Pablo Pardo, Guillermo Mendoza-Hernández, Federico MartÃnez, Oscar Flores-Herrera,