scholarly journals ATP Synthesis Catalyzed by the ATP Synthase of Escherichia coli Reconstituted into Liposomes

1994 ◽  
Vol 225 (1) ◽  
pp. 167-172 ◽  
Author(s):  
Susanne Fischer ◽  
Carsten Etzold ◽  
Paola Turina ◽  
Gabriele Deckers-Hebestreit ◽  
Karlheinz Altendorf ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Atp Synthesis

scholarly journals Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase

2015 ◽  
Vol 290 (34) ◽  
pp. 21032-21041 ◽  
Author(s):  
Naman B. Shah ◽  
Thomas M. Duncan
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Atp Hydrolysis ◽  
Atp Synthesis ◽  
Intrinsic Rate ◽  
Synthesis Rate ◽  
Final Segment ◽  
Rotary Catalysis

F-type ATP synthases are rotary nanomotor enzymes involved in cellular energy metabolism in eukaryotes and eubacteria. The ATP synthase from Gram-positive and -negative model bacteria can be autoinhibited by the C-terminal domain of its ϵ subunit (ϵCTD), but the importance of ϵ inhibition in vivo is unclear. Functional rotation is thought to be blocked by insertion of the latter half of the ϵCTD into the central cavity of the catalytic complex (F1). In the inhibited state of the Escherichia coli enzyme, the final segment of ϵCTD is deeply buried but has few specific interactions with other subunits. This region of the ϵCTD is variable or absent in other bacteria that exhibit strong ϵ-inhibition in vitro. Here, genetically deleting the last five residues of the ϵCTD (ϵΔ5) caused a greater defect in respiratory growth than did the complete absence of the ϵCTD. Isolated membranes with ϵΔ5 generated proton-motive force by respiration as effectively as with wild-type ϵ but showed a nearly 3-fold decrease in ATP synthesis rate. In contrast, the ϵΔ5 truncation did not change the intrinsic rate of ATP hydrolysis with membranes. Further, the ϵΔ5 subunit retained high affinity for isolated F1 but reduced the maximal inhibition of F1-ATPase by ϵ from >90% to ∼20%. The results suggest that the ϵCTD has distinct regulatory interactions with F1 when rotary catalysis operates in opposite directions for the hydrolysis or synthesis of ATP.

Turnover Number of Escherichia coli F0F1 ATP Synthase for ATP Synthesis in Membrane Vesicles

1997 ◽  
Vol 243 (1-2) ◽  
pp. 336-343 ◽  
Author(s):  
Carsten Etzold ◽  
Gabriele Deckers-Hebestreit ◽  
Karlheinz Altendorf
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Atp Synthesis ◽  
Membrane Vesicles ◽  
Turnover Number ◽  
F0f1 Atp Synthase

scholarly journals ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase

2008 ◽  
Vol 1777 (1) ◽  
pp. 32-38 ◽  
Author(s):  
Robert R. Ishmukhametov ◽  
J. Blake Pond ◽  
Asma Al-Huqail ◽  
Mikhail A. Galkin ◽  
Steven B. Vik
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Atp Synthesis ◽  
Subunit A

Assembly of the Escherichia coli FoF1 ATP synthase involves distinct subcomplex formation

2013 ◽  
Vol 41 (5) ◽  
pp. 1288-1293 ◽  
Author(s):  
Gabriele Deckers-Hebestreit
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Cytoplasmic Membrane ◽  
Atp Synthesis ◽  
E Coli ◽  
Assembly Pathway ◽  
Polypeptide Chains ◽  
Fof1 Atp Synthase

The ATP synthase (FoF1) of Escherichia coli couples the translocation of protons across the cytoplasmic membrane by Fo to ATP synthesis or hydrolysis in F1. Whereas good knowledge of the nanostructure and the rotary mechanism of the ATP synthase is at hand, the assembly pathway of the 22 polypeptide chains present in a stoichiometry of ab2c10α3β3γδϵ has so far not received sufficient attention. In our studies, mutants that synthesize different sets of FoF1 subunits allowed the characterization of individually formed stable subcomplexes. Furthermore, the development of a time-delayed in vivo assembly system enabled the subsequent synthesis of particular missing subunits to allow the formation of functional ATP synthase complexes. These observations form the basis for a model that describes the assembly pathway of the E. coli ATP synthase from pre-formed subcomplexes, thereby avoiding membrane proton permeability by a concomitant assembly of the open H+-translocating unit within a coupled FoF1 complex.

scholarly journals Rates of various reactions catalyzed by ATP synthase as related to the mechanism of ATP synthesis.

1991 ◽  
Vol 266 (1) ◽  
pp. 123-129
Author(s):  
D A Berkich ◽  
G D Williams ◽  
P T Masiakos ◽  
M B Smith ◽  
P D Boyer ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Atp Synthesis

scholarly journals Carbon and Nitrogen Sources Have No Impact on the Organization and Composition of Ustilago maydis Respiratory Supercomplexes

2021 ◽  
Vol 7 (1) ◽  
pp. 42
Author(s):  
Deyamira Matuz-Mares ◽  
Oscar Flores-Herrera ◽  
Guadalupe Guerra-Sánchez ◽  
Lucero Romero-Aguilar ◽  
Héctor Vázquez-Meza ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Atp Synthesis ◽  
Nitrogen Sources ◽  
Growth Conditions ◽  
Energy Conditions ◽  
Respiratory Complexes ◽  
Respiratory Supercomplexes ◽  
Nadh Dehydrogenases ◽  
Reduced Nicotinamide Adenine Dinucleotide

Respiratory supercomplexes are found in mitochondria of eukaryotic cells and some bacteria. A hypothetical role of these supercomplexes is electron channeling, which in principle should increase the respiratory chain efficiency and ATP synthesis. In addition to the four classic respiratory complexes and the ATP synthase, U. maydis mitochondria contain three type II NADH dehydrogenases (NADH for reduced nicotinamide adenine dinucleotide) and the alternative oxidase. Changes in the composition of the respiratory supercomplexes due to energy requirements have been reported in certain organisms. In this study, we addressed the organization of the mitochondrial respiratory complexes in U. maydis under diverse energy conditions. Supercomplexes were obtained by solubilization of U. maydis mitochondria with digitonin and separated by blue native polyacrylamide gel electrophoresis (BN-PAGE). The molecular mass of supercomplexes and their probable stoichiometries were 1200 kDa (I1:IV1), 1400 kDa (I1:III2), 1600 kDa (I1:III2:IV1), and 1800 kDa (I1:III2:IV2). Concerning the ATP synthase, approximately half of the protein is present as a dimer and half as a monomer. The distribution of respiratory supercomplexes was the same in all growth conditions. We did not find evidence for the association of complex II and the alternative NADH dehydrogenases with other respiratory complexes.

Sign in / Sign up

Export Citation Format

Share Document