Cited by 614ATP Synthase and ATPases ResearchPhotosynthetic Processes and MechanismsMitochondrial Function and Pathology

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The ATP synthase: the understood, the uncertain and the unknown

Walker, John E.·2013·Biochemical Society Transactions

DOI 10.1042/bst20110773

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Abstract

The ATP synthases are multiprotein complexes found in the energy-transducing membranes of bacteria, chloroplasts and mitochondria. They employ a transmembrane protonmotive force, Δp, as a source of energy to drive a mechanical rotary mechanism that leads to the chemical synthesis of ATP from ADP and Pi. Their overall architecture, organization and mechanistic principles are mostly well established, but other features are less well understood. For example, ATP synthases from bacteria, mitochondria and chloroplasts differ in the mechanisms of regulation of their activity, and the molecular bases of these different mechanisms and their physiological roles are only just beginning to emerge. Another crucial feature lacking a molecular description is how rotation driven by Δp is generated, and how rotation transmits energy into the catalytic sites of the enzyme to produce the stepping action during rotation. One surprising and incompletely explained deduction based on the symmetries of c-rings in the rotor of the enzyme is that the amount of energy required by the ATP synthase to make an ATP molecule does not have a universal value. ATP synthases from multicellular organisms require the least energy, whereas the energy required to make an ATP molecule in unicellular organisms and chloroplasts is higher, and a range of values has been calculated. Finally, evidence is growing for other roles of ATP synthases in the inner membranes of mitochondria. Here the enzymes form supermolecular complexes, possibly with specific lipids, and these complexes probably contribute to, or even determine, the formation of the cristae.

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Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
Abrahams, J., Leslie, A. G., Lutter, R., & Walker, J. (1994) · Nature · doi:10.1038/370621a0 · Cited by 2,961
Self-citation
Direct observation of the rotation of F1-ATPase
Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (1997) · Nature · doi:10.1038/386299a0 · Cited by 2,216
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,102
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,019
RESPIRATORY ENZYMES IN OXIDATIVE PHOSPHORYLATION
Chance, B., & Williams, G. R. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57189-7 · Cited by 1,473
Molecular Architecture of the Rotary Motor in ATP Synthase
Stock, D., Leslie, A. G. W., & Walker, J. E. (1999) · Science · doi:10.1126/science.286.5445.1700 · Cited by 1,271
Self-citation
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
The binding change mechanism for ATP synthase--some probabilities and possibilities.
Boyer, P. (1993) · Biochimica et Biophysica Acta · doi:10.1016/0005-2728(93)90063-l · Cited by 968
Architecture of succinate dehydrogenase and reactive oxygen species generation
Yankovskaya, V., Horsefield, R., Törnroth, S., Luna-Chavez, C., Miyoshi, H., Léger, C., Byrne, B., Cecchini, G., & Iwata, S. (2003) · Science · doi:10.1126/science.1079605 · Cited by 927
Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II
Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M., & Rao, Z. (2005) · Cell · doi:10.1016/j.cell.2005.05.025 · Cited by 881

Show all 123 references

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Authors: Walker, J. E.
Affiliations: MRC Mitochondrial Biology Unit (GB)
Corresponding author: Walker, John E.
ORCID: Walker, John E.
Venue: Biochemical Society Transactions
Publisher: Portland Press Ltd.
Published: 2013-01-29
Volume: 41
Issue: 1
Pages: 1-16
ISSN: 0300-5127 (ISSN-L)
1470-8752
DOI: 10.1042/bst20110773
OpenAlex: W2104675030
Cited by: 614
References: 123
Citations by year: 2026: 39 · 2025: 44 · 2024: 48 · 2023: 39 · 2022: 47 · 2021: 56 · 2020: 61 · 2019: 46 · 2018: 52 · 2017: 42 · 2016: 42 · 2015: 54 · 2014: 30 · 2013: 13
FWCI: 4.36
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Society Transactions (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: ATP synthase, proton motive force, rotary mechanism, ATP production, enzyme regulation, mitochondrial ATP synthase, chloroplast ATP synthase, bacterial ATP synthase, supramolecular complexes
MeSH terms: Hydrolysis, Models, Molecular, Protein Conformation, ATP Synthetase Complexes, Uncertainty

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The ATP synthase: the understood, the uncertain and the unknown

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