Functional production of the Na+ F1FO ATP synthase from Acetobacterium woodii in Escherichia coli requires the native AtpI

2012 ◽  
Vol 45 (1-2) ◽  
pp. 15-23 ◽  
Author(s):  
Karsten Brandt ◽  
Daniel B. Müller ◽  
Jan Hoffmann ◽  
Christine Hübert ◽  
Bernd Brutschy ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Acetobacterium Woodii ◽  
F1fo Atp Synthase

scholarly journals A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase

2006 ◽  
Vol 1757 (3) ◽  
pp. 206-214 ◽  
Author(s):  
Mikhail A. Galkin ◽  
Robert R. Ishmukhametov ◽  
Steven B. Vik
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
F1fo Atp Synthase

Production of fully assembled and active Aquifex aeolicus F1FO ATP synthase in Escherichia coli

2014 ◽  
Vol 1840 (1) ◽  
pp. 34-40 ◽  
Author(s):  
Chunli Zhang ◽  
Matteo Allegretti ◽  
Janet Vonck ◽  
Julian D. Langer ◽  
Marco Marcia ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Aquifex Aeolicus ◽  
F1fo Atp Synthase

scholarly journals Expression, purification and crystallization of central stalk and peripheral stalk of F1Fo ATP synthase from Aquifex aeolicus in Escherichia coli

2012 ◽  
Vol 1817 ◽  
pp. S27
Author(s):  
Shuai Xin ◽  
Chunli Zhang ◽  
Julian Langer ◽  
Guohong Peng ◽  
Hartmut Michel
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Aquifex Aeolicus ◽  
F1fo Atp Synthase ◽  
Peripheral Stalk ◽  
Central Stalk

The b arg36 contributes to efficient coupling in F1FO ATP synthase in Escherichia coli

2008 ◽  
Vol 40 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Amanda K. Welch ◽  
Shane B. Claggett ◽  
Brian D. Cain
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
F1fo Atp Synthase ◽  
Efficient Coupling

scholarly journals Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1Fo ATP synthase

2005 ◽  
Vol 1706 (1-2) ◽  
pp. 110-116 ◽  
Author(s):  
Robert R. Ishmukhametov ◽  
Mikhail A. Galkin ◽  
Steven B. Vik
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
F1fo Atp Synthase

scholarly journals Clostridium pasteurianum F1Fo ATP Synthase: Operon, Composition, and Some Properties

2003 ◽  
Vol 185 (18) ◽  
pp. 5527-5535 ◽  
Author(s):  
Amaresh Das ◽  
Lars G. Ljungdahl
Keyword(s):  
Escherichia Coli ◽  
Atpase Activity ◽  
Atp Synthase ◽  
Reverse Transcription ◽  
Anaerobic Bacterium ◽  
Clostridium Pasteurianum ◽  
F1fo Atp Synthase ◽  
Reverse Transcription Pcr ◽  
Obligate Anaerobic ◽  
Sulfhydryl Compounds

ABSTRACT The atp operon encoding F1Fo ATP synthase in the fermentative obligate anaerobic bacterium Clostridium pasteurianum was sequenced. It consisted of nine genes arranged in the order atpI(i), atpB(a), atpE(c), atpF(b), atpH(δ), atpA(α), atpG(γ), atpD(β), and atpC(ε), which was identical to that found in many bacteria. Reverse transcription-PCR confirmed the presence of the transcripts of all nine genes. The amount of ATPase activity in the membranes of C. pasteurianum was low compared to what has been found in many other bacteria. The F1Fo complexes solubilized from membranes of C. pasteurianum and Escherichia coli had similar masses, suggesting similar compositions for the F1Fo complexes from the two bacteria. Western blotting experiments with antibodies raised against the purified subunits of F1Fo detected the presence of eight subunits, α, β, γ, δ, ε, a, b, and c, in the F1Fo complex from C. pasteurianum. The F1Fo complex from C. pasteurianum was activated by thiocyanate, cyanate, or sulfhydryl compounds; inhibited by sulfite, bisulfite, or bicarbonate; and had tolerance to inhibition by dicyclohexylcarbodiimide. The target of thiol activation of the F1Fo complex from C. pasteurianum was F1. Thiocyanate and sulfite were noncompetitive with respect to substrate Mg ATP but competitive with respect to each other. The F1 and Fo parts of the F1Fo complexes from C. pasteurianum and E. coli bound to each other, but the hybrid F1Fo complexes were not functionally active.

Low resolution structure of subunit b (b 22–156) of Escherichia coli F1FO ATP synthase in solution and the b−δ assembly

2008 ◽  
Vol 40 (4) ◽  
pp. 245-255 ◽  
Author(s):  
Ragunathan Priya ◽  
Vikeramjeet S. Tadwal ◽  
Manfred W. Roessle ◽  
Shovanlal Gayen ◽  
Cornelia Hunke ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Low Resolution ◽  
F1fo Atp Synthase ◽  
Subunit B ◽  
Resolution Structure

scholarly journals Half channels mediating H+ transport and the mechanism of gating in the Fo sector of Escherichia coli F1Fo ATP synthase

2014 ◽  
Vol 1837 (7) ◽  
pp. 1063-1068 ◽  
Author(s):  
Robert H. Fillingame ◽  
P. Ryan Steed
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
F1fo Atp Synthase
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