The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Structure and Mechanisms of F-Type ATP Synthases
Abstract
F 1 F o ATP synthases produce most of the ATP in the cell. F-type ATP synthases have been investigated for more than 50 years, but a full understanding of their molecular mechanisms has become possible only with the recent structures of complete, functionally competent complexes determined by electron cryo-microscopy (cryo-EM). High-resolution cryo-EM structures offer a wealth of unexpected new insights. The catalytic F 1 head rotates with the central γ -subunit for the first part of each ATP-generating power stroke. Joint rotation is enabled by subunit δ/OSCP acting as a flexible hinge between F 1 and the peripheral stalk. Subunit a conducts protons to and from the c -ring rotor through two conserved aqueous channels. The channels are separated by ∼6 Å in the hydrophobic core of F o , resulting in a strong local field that generates torque to drive rotary catalysis in F 1 . The structure of the chloroplast F 1 F o complex explains how ATPase activity is turned off at night by a redox switch. Structures of mitochondrial ATP synthase dimers indicate how they shape the inner membrane cristae. The new cryo-EM structures complete our picture of the ATP synthases and reveal the unique mechanism by which they transform an electrochemical membrane potential into biologically useful chemical energy.
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Citations
Cites
Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325
Self-citationHohmann-Marriott, M. F., & Blankenship, R. E. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042110-103811 · Cited by 744
The ATP synthase: the understood, the uncertain and the unknown
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Oligomycin Frames a Common Drug-Binding Site in the ATP Synthase
Symersky, J., Osowski, D., Walters, D. E., & Mueller, D. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207912109 · Cited by 269
Atomic model for the dimeric F O region of mitochondrial ATP synthase
Guo, H., Bueler, S. A., & Rubinstein, J. L. (2017) · Science · doi:10.1126/science.aao4815 · Cited by 225
Inventing the dynamo machine: the evolution of the F-type and V-type ATPases
Mulkidjanian, A. Y., Makarova, K. S., Galperin, M. Y., & Koonin, E. V. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1767 · Cited by 210
ATP synthases from archaea: The beauty of a molecular motor
Grüber, G., Manimekalai, M. S. S., Mayer, F., & Müller, V. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.03.004 · Cited by 140
ATP Synthase Diseases of Mitochondrial Genetic Origin
Dautant, A., Meier, T., Hahn, A., Tribouillard-Tanvier, D., di Rago, J.-P., & Kucharczyk, R. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00329 · Cited by 127
One step beyond a ribosome: The ancient anaerobic core
Sousa, F. L., Nelson-Sathi, S., & Martin, W. F. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.04.284 · Cited by 58
Cited by
Cellular ATP demand creates metabolically distinct subpopulations of mitochondria
Ryu, K. W., Fung, T. S., Baker, D. C., Saoi, M., Park, J., Febres-Aldana, C. A., Aly, R. G., Cui, R., Sharma, A., Fu, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-08146-w · Cited by 284
In-cell architecture of the mitochondrial respiratory chain
Waltz, F., Righetto, R. D., Lamm, L., Salinas-Giegé, T., Kelley, R., Zhang, X., Obr, M., Khavnekar, S., Kotecha, A., & Engel, B. D. (2025) · Science · doi:10.1126/science.ads8738 · Cited by 95
ATP synthase evolution on a cross-braced dated tree of life
Mahendrarajah, T. A., Moody, E. R. R., Schrempf, D., Szánthó, L. L., Dombrowski, N., Davín, A. A., Pisani, D., Donoghue, P. C. J., Szöllősi, G. J., Williams, T. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42924-w · Cited by 86
“F-type ATP synthases are ubiquitous across bacteria and eukaryotes and localize to cellular, mitochondrial, and plastid membranes 39 .”
BackgroundCarraro, M., Carrer, A., Urbani, A., & Bernardi, P. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.05.014 · Cited by 71
Benzerara, K., Duprat, E., Bitard-Feildel, T., Caumes, G., Cassier-Chauvat, C., Chauvat, F., Dezi, M., Diop, S. I., Gaschignard, G., Görgen, S., et al. (2022) · Genome Biology and Evolution · doi:10.1093/gbe/evac026 · Cited by 47
Current understanding of structure, function and biogenesis of yeast mitochondrial ATP synthase
Artika, I. M. (2019) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-019-09809-4 · Cited by 24
An NADH-controlled gatekeeper of ATP synthase
Schildhauer, F., Ryl, P. S. J., Lauer, S. M., Lenz, S., Barlas, A. B., Ouzounidis, V. R., Jeffrey, K., Marcu, D.-C., O’Reilly, F. J., Graziadei, A., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.06.007 · Cited by 11
Bile resistance mechanisms in probiotics: From structural adaptation to metabolic regulation
Hu, J.-W., Guo, S.-J., Zhang, L.-W., & Guo, C.-F. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.108282 · Cited by 5
Wong, J. E., Zíková, A., & Gahura, O. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad146 · Cited by 3
Metadata
- Authors
- Kühlbrandt, W.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2019-06-20
- Volume
- 88
- Issue
- 1
- Pages
- 515-549
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2925284108
- Cited by
- 444
- References
- 9
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- closed
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