scholarly journals An ATP synthase harboring an atypical γ-subunit is involved in ATP synthesis in tomato fruit chromoplasts

2013 ◽  
Vol 74 (1) ◽  
pp. 74-85 ◽  
Author(s):  
Irini Pateraki ◽  
Marta Renato ◽  
Joaquín Azcón-Bieto ◽  
Albert Boronat
Keyword(s):  
Atp Synthase ◽  
Tomato Fruit ◽  
Atp Synthesis ◽  
Γ Subunit

scholarly journals ATP Synthase with Its γ Subunit Reduced to the N-terminal Helix Can Still Catalyze ATP Synthesis

2009 ◽  
Vol 284 (39) ◽  
pp. 26519-26525 ◽  
Author(s):  
Nelli Mnatsakanyan ◽  
Jonathon A. Hook ◽  
Leah Quisenberry ◽  
Joachim Weber
Keyword(s):  
Atp Synthase ◽  
Atp Synthesis ◽  
Γ Subunit

scholarly journals The phototroph-specific β-hairpin structure of the γ subunit of FoF1-ATP synthase is important for efficient ATP-synthesis of cyanobacteria

2021 ◽  
pp. 101027
Author(s):  
Kumiko Kondo ◽  
Masayuki Izumi ◽  
Kosuke Inabe ◽  
Keisuke Yoshida ◽  
Mari Imashimizu ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Atp Synthesis ◽  
Hairpin Structure ◽  
Γ Subunit ◽  
Fof1 Atp Synthase

C-Terminal Mutations in the Chloroplast ATP Synthase γ Subunit Impair ATP Synthesis and Stimulate ATP Hydrolysis†

Biochemistry ◽  
2008 ◽  
Vol 47 (2) ◽  
pp. 836-844 ◽  
Author(s):  
Feng He ◽  
Hardeep S. Samra ◽  
Eric A. Johnson ◽  
Nicholas R. Degner ◽  
Richard E. McCarty ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Atp Hydrolysis ◽  
Atp Synthesis ◽  
Chloroplast Atp Synthase ◽  
Γ Subunit

Stepwise rotation of the γ-subunit of EF o F 1 -ATP synthase during ATP synthesis: a single-molecule FRET approach

2003 ◽  
Author(s):  
Michael Borsch ◽  
Manuel Diez ◽  
Boris Zimmermann ◽  
Matthias Trost ◽  
Stefan Steigmiller ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Single Molecule ◽  
Atp Synthesis ◽  
Single Molecule Fret ◽  
Γ Subunit

scholarly journals Structural basis of redox modulation on chloroplast ATP synthase

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Jay-How Yang ◽  
Dewight Williams ◽  
Eaazhisai Kandiah ◽  
Petra Fromme ◽  
Po-Lin Chiu
Keyword(s):  
Atp Synthase ◽  
Higher Plants ◽  
Atp Synthesis ◽  
Smooth Transition ◽  
Structural Basis ◽  
Energy Regulation ◽  
Redox Modulation ◽  
Disulfide Linkage ◽  
Chloroplast Atp Synthase ◽  
Γ Subunit

AbstractIn higher plants, chloroplast ATP synthase has a unique redox switch on its γ subunit that modulates enzyme activity to limit ATP hydrolysis at night. To understand the molecular details of the redox modulation, we used single-particle cryo-EM to determine the structures of spinach chloroplast ATP synthase in both reduced and oxidized states. The disulfide linkage of the oxidized γ subunit introduces a torsional constraint to stabilize the two β hairpin structures. Once reduced, free cysteines alleviate this constraint, resulting in a concerted motion of the enzyme complex and a smooth transition between rotary states to facilitate the ATP synthesis. We added an uncompetitive inhibitor, tentoxin, in the reduced sample to limit the flexibility of the enzyme and obtained high-resolution details. Our cryo-EM structures provide mechanistic insight into the redox modulation of the energy regulation activity of chloroplast ATP synthase.

scholarly journals ECS-based investigation of chloroplast ATP synthase regulation

2020 ◽  
Author(s):  
Felix Buchert ◽  
Benjamin Bailleul ◽  
Pierre Joliot
Keyword(s):  
Atp Synthase ◽  
Redox Regulation ◽  
Spectroscopic Method ◽  
Atp Synthesis ◽  
Redox States ◽  
Chloroplast Atp Synthase ◽  
Γ Subunit ◽  
Synthase Regulation

AbstractThe chloroplast ATP synthase (CF1Fo) contains a specific feature to the green lineage: a γ-subunit redox domain which contains a cysteine couple and interacts with the torque-generating βDELSEED-loop. Based on the recently solved structure of this domain, it was proposed to function as a chock. In vitro, γ-disulfide formation slows down the activity of the CF1Fo at low transmembrane electrochemical proton gradient . Here, we utilize in vivo absorption spectroscopy measurements for functional CF1Fo activity characterization in Arabidopsis leaves. The spectroscopic method allows us to measure the present in dark-adapted leaves, and to identify its mitochondrial sources. Furthermore, we follow the fate of the extra generated by an illumination, including its osmotic and electric components, and from there we estimate the lifetime of the light-generated ATP. In contrast with a previous report [Joliot and Joliot, Biochim. Biophys. Acta, 1777 (2008) 676-683], the CF1Fo γ-subunit exists mostly in an oxidized form in the dark-adapted state. To study the redox regulation of the CF1Fo, we used thiol agent infiltration in WT and a mutant that does not form the γ-disulfide. The obtained -dependent CF1Fo activity profile in the two γ-redox states in vivo reconciles with previous biochemical in vitro findings [Junesch and Gräber, Biochim. Biophys. Acta, 893 (1987) 275-288]. The highest rates of ATP synthesis we measured in the two γ-redox state were similar at high . In the presence of the γ-dithiol, similar rates were obtained at a ~45 mV lower value compared to the oxidized state, which closely resembled the energetic gap of 0.7 ΔpH units reported in vitro.

scholarly journals Two genes, atpC1 and atpC2, for the γ subunit of Arabidopsis thaliana chloroplast ATP synthase

1991 ◽  
Vol 266 (12) ◽  
pp. 7333-7338
Author(s):  
N Inohara ◽  
A Iwamoto ◽  
Y Moriyama ◽  
S Shimomura ◽  
M Maeda ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Atp Synthase ◽  
Chloroplast Atp Synthase ◽  
Γ Subunit

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.

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