Disentangling chloroplast ATP synthase regulation by proton motive force and thiol modulation in Arabidopsis leaves

2021 ◽  
pp. 148434
Author(s):  
Felix Buchert ◽  
Benjamin Bailleul ◽  
Pierre Joliot
Keyword(s):  
Atp Synthase ◽  
Proton Motive Force ◽  
Motive Force ◽  
Chloroplast Atp Synthase ◽  
Synthase Regulation

scholarly journals The Activity of the ATP Synthase fromEscherichia coliIs Regulated by the Transmembrane Proton Motive Force

2000 ◽  
Vol 275 (39) ◽  
pp. 30157-30162 ◽  
Author(s):  
Susanne Fischer ◽  
Peter Gräber ◽  
Paola Turina
Keyword(s):  
Atp Synthase ◽  
Proton Motive Force ◽  
Motive Force

scholarly journals Is Myelin a Mitochondrion?

2012 ◽  
Vol 33 (1) ◽  
pp. 33-36 ◽  
Author(s):  
Julia J Harris ◽  
David Attwell
Keyword(s):  
Membrane Potential ◽  
Respiratory Chain ◽  
Atp Synthase ◽  
Proton Motive Force ◽  
Motive Force ◽  
Myelin Membrane ◽  
Considerable Doubt

It has been hypothesized that myelin acts like a mitochondrion, generating ATP across the membranes of its sheath. By calculating the proton motive force across the myelin membrane based on known values for the pH and membrane potential of the oligodendrocyte, we find that insufficient energy could be harvested from proton flow across the myelin membrane to synthesize ATP. In fact, if the respiratory chain were present in the myelin membrane, then the ATP synthase would function in reverse, hydrolyzing rather than synthesizing ATP. This calculation places the hypothesis of an energy-producing role for myelin in considerable doubt.

scholarly journals Biased Brownian stepping rotation of FoF1-ATP synthase driven by proton motive force

2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Rikiya Watanabe ◽  
Kazuhito V. Tabata ◽  
Ryota Iino ◽  
Hiroshi Ueno ◽  
Masayuki Iwamoto ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Proton Motive Force ◽  
Motive Force ◽  
Fof1 Atp Synthase

scholarly journals Chloroplastic ATP synthase builds up a proton motive force preventing production of reactive oxygen species in photosystem I

2017 ◽  
Vol 91 (2) ◽  
pp. 306-324 ◽  
Author(s):  
Daisuke Takagi ◽  
Katsumi Amako ◽  
Masaki Hashiguchi ◽  
Hidehiro Fukaki ◽  
Kimitsune Ishizaki ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Atp Synthase ◽  
Photosystem I ◽  
Reactive Oxygen ◽  
Proton Motive Force ◽  
Motive Force ◽  
Oxygen Species

scholarly journals Direct Observation of the Rotary Motion of FOF1-ATP Synthase Driven by Proton Motive Force

2013 ◽  
Vol 104 (2) ◽  
pp. 277a
Author(s):  
Rikiya Watanabe ◽  
Kazuhito V. Tabata ◽  
Ryota Iino ◽  
Hiroyuki Noji
Keyword(s):  
Atp Synthase ◽  
Direct Observation ◽  
Proton Motive Force ◽  
Motive Force ◽  
Rotary Motion ◽  
Fof1 Atp Synthase

scholarly journals Mitochondrial F1FO ATP synthase determines the local proton motive force in cristae tips

2021 ◽  
Author(s):  
Bettina Rieger ◽  
Tasnim Arroum ◽  
Jimmy Villalta ◽  
Karin B. Busch
Keyword(s):  
Atp Synthase ◽  
Mammalian Cells ◽  
Atp Hydrolysis ◽  
Ph Sensor ◽  
Atp Synthesis ◽  
Proton Motive Force ◽  
Motive Force ◽  
List Type ◽  
Inner Mitochondrial Membrane ◽  
Respiratory Chain Complexes

ABSTRACTThe classical view of oxidative phosphorylation is that a proton motive force PMF generated by the respiratory chain complexes fuels ATP synthesis. Under glycolytic conditions, ATP synthase in its reverse mode also can contribute to the PMF. Here, we dissected the two functions of ATP synthase and the role of its inhibitory factor 1 (IF1) under different metabolic conditions in detail. pH profiles of mitochondrial sub-compartments were recorded with high spatial resolution in live mammalian cells by positioning a pH-sensor directly at F1 and FO of ATP synthase, complex IV and in the matrix. Our results clearly show that ATP synthase activity is substantially controlling the PMF and that IF1 is essential under OXPHOS conditions to prevent reverse ATP synthase activity due to an almost negligible ΔpH.GRAPHICAL ABSTRACTHIGHLIGHTSThe ΔpH along and across the inner mitochondrial membrane is not homogeneousThe proton motive force at cristae tips is controlled by F1 FO ATP synthaseUnder OXPHOS conditions, the pH difference between FO and F1 of active ATP synthase is almost negligible (1.2 proton vs. 1 proton equivalent)IF1 is required to prevent the onset of ATP hydrolysis under OXPHOS conditions

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