ReviewThe Journal of membrane biology2015
Opposite rotation directions in the synthesis and hydrolysis of ATP by the ATP synthase: hints from a subunit asymmetry.
Review in The Journal of membrane biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Reflecting on chiral chimeric cancer and microbes: ambidextrous metabolism-the real danger?Frontiers in cell and developmental biology · 2025Article
- Evaluating the mitochondrial structure and gene expression profile of regenerated liver tissues in mice after 85% partial hepatectomy.Journal of gastrointestinal oncology · 2024Article
- Energy Regulation in Inflammatory Sarcopenia by the Purinergic System.International journal of molecular sciences · 2023Review
- Inhibition of ATP synthase reverse activity restores energy homeostasis in mitochondrial pathologies.The EMBO journal · 2023Article
- From the Structural and (Dys)Function of ATP Synthase to Deficiency in Age-Related Diseases.Life (Basel, Switzerland) · 2022Review
- Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology.Life (Basel, Switzerland) · 2021Review
- Modularize and Unite: Toward Creating a Functional Artificial Cell.Frontiers in molecular biosciences · 2021Review
- Differential Proteomics Analysis of the Subcutaneous Connective Tissues in Alcian Blue Tracks along Conception Vessel and Adjacent Nonmeridian in Rats.Evidence-based complementary and alternative medicine : eCAM · 2021Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Selective ATP hydrolysis inhibition in F1Fo ATP synthase enhances radiosensitivity in non-small-cell lung cancer cells (A549).Oncotarget · 2017Article
- The c-Ring of the F1FO-ATP Synthase: Facts and Perspectives.The Journal of membrane biology · 2016Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ATP synthase can be imagined as a reversible H(+)-translocating channel embedded in the membrane, FO portion, coupled to a protruding catalytic portion, F1. Under physiological conditions the F1FO complex synthesizes ATP by exploiting the transmembrane electrochemical gradient of protons and their downhill movement. Alternatively, under other patho-physiological conditions it exploits ATP hydrolysis to energize the membrane by uphill pumping protons. The reversibility of the mechanism is guaranteed by the structural coupling between the hydrophilic F1 and the hydrophobic FO. Which of the two opposite processes wins in the energy-transducing membrane complex depends on the thermodynamic balance between the protonmotive force (Δp) and the phosphorylation potential of ATP (ΔG P). Accordingly, while Δp prevalence drives ATP synthesis by translocating protons from the membrane P-side to the N-side and generating anticlockwise torque rotation (viewed from the matrix), ΔG P drives ATP hydrolysis by chemomechanical coupling of FO to F1 with clockwise torque. The direction of rotation is the same in all the ATP synthases, due to the conserved steric arrangement of the chiral a subunit of FO. The ability of this coupled bi-functional complex to produce opposite rotations in ATP synthesis and hydrolysis is explained on the basis of the a subunit asymmetry.
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Registered trials
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