کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8298711 | 1537041 | 2015 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The a subunit of the A1AO ATP synthase of Methanosarcina mazei Gö1 contains two conserved arginine residues that are crucial for ATP synthesis
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کلمات کلیدی
DCCDpsigIMVSdithioerythritolisopropyl-β-d-1-thiogalactopyranosideDTEIPTGDDMn-Dodecyl-β-D-maltoside - n-Dodecyl-β-D-مالتوزیدN,N′-dicyclohexylcarbodiimide - N، N'-dicyclohexylcarbodiimideDES - ازArchaea - باستانیان یا آرکیاEnergy conservation - حفاظت از انرژیDiethylstilbestrol - دی اتیلستیل بسترولSite directed mutagenesis - سایت موتاگنسیس را هدایت می کندMethanogens - متان ژن هاIon translocation - نقل مکان یون
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: The a subunit of the A1AO ATP synthase of Methanosarcina mazei Gö1 contains two conserved arginine residues that are crucial for ATP synthesis The a subunit of the A1AO ATP synthase of Methanosarcina mazei Gö1 contains two conserved arginine residues that are crucial for ATP synthesis](/preview/png/8298711.png)
چکیده انگلیسی
Like the evolutionary related F1FO ATP synthases and V1VO ATPases, the A1AO ATP synthases from archaea are multisubunit, membrane-bound transport machines that couple ion flow to the synthesis of ATP. Although the subunit composition is known for at least two species, nothing is known so far with respect to the function of individual subunits or amino acid residues. To pave the road for a functional analysis of A1AO ATP synthases, we have cloned the entire operon from Methanosarcina mazei into an expression vector and produced the enzyme in Escherichia coli. Inverted membrane vesicles of the recombinants catalyzed ATP synthesis driven by NADH oxidation as well as artificial driving forces. ÎμËH+ as well as ÎpH were used as driving forces which is consistent with the inhibition of NADH-driven ATP synthesis by protonophores. Exchange of the conserved glutamate in subunit c led to a complete loss of ATP synthesis, proving that this residue is essential for H+ translocation. Exchange of two conserved arginine residues in subunit a has different effects on ATP synthesis. The role of these residues in ion translocation is discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1847, Issues 6â7, JuneâJuly 2015, Pages 505-513
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1847, Issues 6â7, JuneâJuly 2015, Pages 505-513
نویسندگان
Carolin Gloger, Anna-Katharina Born, Martin Antosch, Volker Müller,