The C-Terminal Domain of the ε Subunit of the Chloroplast ATP Synthase Is Not Required for ATP Synthesis†

Biochemistry ◽  
2002 ◽  
Vol 41 (51) ◽  
pp. 15130-15134 ◽  
Author(s):  
Kristine F. Nowak ◽  
Vazha Tabidze ◽  
Richard E. McCarty
Keyword(s):  
Atp Synthase ◽  
Atp Synthesis ◽  
Chloroplast Atp Synthase ◽  
Terminal Domain

Kinetics of Proton-Transport-Coupled ATP Synthesis Catalyzed by the Chloroplast ATP Synthase

1986 ◽  
Vol 90 (11) ◽  
pp. 1034-1040 ◽  
Author(s):  
P. Gräber ◽  
P. Fromme ◽  
U. Junesch ◽  
G. Schmidt ◽  
G. Thulke
Keyword(s):  
Atp Synthase ◽  
Proton Transport ◽  
Atp Synthesis ◽  
Chloroplast Atp Synthase ◽  
Kinetics Of

scholarly journals Feedback limitation of photosynthesis at high CO2 acts by modulating the activity of the chloroplast ATP synthase

2009 ◽  
Vol 36 (11) ◽  
pp. 893 ◽  
Author(s):  
Olavi Kiirats ◽  
Jeffrey A. Cruz ◽  
Gerald E. Edwards ◽  
David M. Kramer
Keyword(s):  
Electron Transfer ◽  
Atp Synthase ◽  
Atp Synthesis ◽  
Nicotiana Sylvestris ◽  
O2 Evolution ◽  
High Co2 ◽  
Chloroplast Atp Synthase ◽  
Low Co2 ◽  
Photosynthetic Electron Transfer

It was previously shown that photosynthetic electron transfer is controlled under low CO2 via regulation of the chloroplast ATP synthase. In the current work, we studied the regulation of photosynthesis under feedback limiting conditions, where photosynthesis is limited by the capacity to utilise triose-phosphate for synthesis of end products (starch or sucrose), in a starch-deficient mutant of Nicotiana sylvestris Speg. & Comes. At high CO2, we observed feedback control that was progressively reversed by increasing O2 levels from 2 to 40%. The activity of the ATP synthase, probed in vivo by the dark-interval relaxation kinetics of the electrochromic shift, was proportional to the O2-induced increases in O2 evolution from PSII (JO2), as well as the sum of Rubisco oxygenation (vo) and carboxylation (vc) rates. The altered ATP synthase activity led to changes in the light-driven proton motive force, resulting in regulation of the rate of plastoquinol oxidation at the cytochrome b6f complex, quantitatively accounting for the observed control of photosynthetic electron transfer. The ATP content of the cell decreases under feedback limitation, suggesting that the ATP synthesis was downregulated to a larger extent than ATP consumption. This likely resulted in slowing of ribulose bisphosphate regeneration and JO2). Overall, our results indicate that, just as at low CO2, feedback limitations control the light reactions of photosynthesis via regulation of the ATP synthase, and can be reconciled with regulation via stromal Pi, or an unknown allosteric affector.

ATP Synthesis Driven by a Valinomycine Induced K+ Diffusion Potential in Liposomes Bearing Chloroplast ATP Synthase

1984 ◽  
Vol 39 (3-4) ◽  
pp. 320-321 ◽  
Author(s):  
M. Dinant ◽  
K. Kaminski
Keyword(s):  
Atp Synthase ◽  
Atp Synthesis ◽  
Diffusion Potential ◽  
Chloroplast Atp Synthase

Partially purified chloroplast ATP synthase was reconstituted into asolectin liposomes. A valinomycine induced potassium diffusion potential from outside to inside the vesicles promoted a measurable ATP synthesis. If valinomycine was replaced by nigericine, practically no ATP was formed

Coupling Proton Movement to ATP Synthesis in the Chloroplast ATP Synthase

2005 ◽  
Vol 37 (6) ◽  
pp. 467-473 ◽  
Author(s):  
Mark L. Richter ◽  
Hardeep S. Samra ◽  
Feng He ◽  
Andrew J. Giessel ◽  
Krzysztof K. Kuczera
Keyword(s):  
Atp Synthase ◽  
Atp Synthesis ◽  
Chloroplast Atp Synthase ◽  
Proton Movement

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

Crucial role of the membrane potential for ATP synthesis by F(1)F(o) ATP synthases

2000 ◽  
Vol 203 (1) ◽  
pp. 51-59 ◽  
Author(s):  
P. Dimroth ◽  
G. Kaim ◽  
U. Matthey
Keyword(s):  
Membrane Potential ◽  
Atp Synthase ◽  
Atp Synthesis ◽  
Operating Conditions ◽  
Chloroplast Atp Synthase ◽  
Counter Rotation ◽  
Cell Energy ◽  
Propionigenium Modestum ◽  
Far From Equilibrium

ATP, the universal carrier of cell energy, is manufactured from ADP and phosphate by the enzyme ATP synthase using the free energy of an electrochemical gradient of protons (or Na(+)). The proton-motive force consists of two components, the transmembrane proton concentration gradient (delta pH) and the membrane potential. The two components were considered to be not only thermodynamically but also kinetically equivalent, since the chloroplast ATP synthase appeared to operate on delta pH only. Recent experiments demonstrate, however, that the chloroplast ATP synthase, like those of mitochondria and bacteria, requires a membrane potential for ATP synthesis. Hence, the membrane potential and proton gradient are not equivalent under normal operating conditions far from equilibrium. These conclusions are corroborated by the finding that only the membrane potential induces a rotary torque that drives the counter-rotation of the a and c subunits in the F(o) motor of Propionigenium modestum ATP synthase.

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