The DOI matches its Crossref record; 82 of the 82 references it cites were found in a registry or an index.
Essentials for ATP Synthesis by F1F0 ATP Synthases
Abstract
The majority of cellular energy in the form of adenosine triphosphate (ATP) is synthesized by the ubiquitous F 1 F 0 ATP synthase. Power for ATP synthesis derives from an electrochemical proton (or Na+) gradient, which drives rotation of membranous F 0 motor components. Efficient rotation not only requires a significant driving force (ΔμH+), consisting of membrane potential (Δψ) and proton concentration gradient (ΔpH), but also a high proton concentration at the source P side. In vivo this is maintained by dynamic proton movements across and along the surface of the membrane. The torque-generating unit consists of the interface of the rotating c ring and the stator a subunit. Ion translocation through this unit involves a sophisticated interplay between the c-ring binding sites, the stator arginine, and the coupling ions on both sides of the membrane. c-ring rotation is transmitted to the eccentric shaft γ-subunit to elicit conformational changes in the catalytic sites of F 1, leading to ATP synthesis.
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Cites
Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
MITCHELL, P. (1961) · Nature · doi:10.1038/191144a0 · Cited by 4,704
CHEMIOSMOTIC COUPLING IN OXIDATIVE AND PHOTOSYNTHETIC PHOSPHORYLATION
MITCHELL, P. (1966) · Biological Reviews · doi:10.1111/j.1469-185x.1966.tb01501.x · Cited by 3,663
Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
Abrahams, J. P., Leslie, A. G. W., Lutter, R., & Walker, J. E. (1994) · Nature · doi:10.1038/370621a0 · Cited by 3,005
Direct observation of the rotation of F1-ATPase
Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (1997) · Nature · doi:10.1038/386299a0 · Cited by 2,236
Oxidative Phosphorylation at the fin de siècle
Saraste, M. (1999) · Science · doi:10.1126/science.283.5407.1488 · Cited by 1,313
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
The binding change mechanism for ATP synthase — Some probabilities and possibilities
Boyer, P. D. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90063-l · Cited by 1,028
Mechanically driven ATP synthesis by F1-ATPase
Itoh, H., Takahashi, A., Adachi, K., Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (2004) · Nature · doi:10.1038/nature02212 · Cited by 545
Energy transduction in ATP synthase
Elston, T., Wang, H., & Oster, G. (1998) · Nature · doi:10.1038/35185 · Cited by 501
ATP formation caused by acid-base transition of spinach chloroplasts.
Jagendorf, A. T., & Uribe, E. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.55.1.170 · Cited by 501
Cited by
Structure and function of mitochondrial membrane protein complexes
Kühlbrandt, W. (2015) · BMC Biology · doi:10.1186/s12915-015-0201-x · Cited by 699
Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. W., & Walker, J. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011099107 · Cited by 513
Schink, B., & Stams, A. J. M. (2013) · The Prokaryotes · doi:10.1007/978-3-642-30123-0_59 · Cited by 371
Bonora, M., Wieckowski, M. R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., & Pinton, P. (2015) · Oncogene · doi:10.1038/onc.2014.96 · Cited by 330
Promiscuous archaeal ATP synthase concurrently coupled to Na + and H + translocation
Schlegel, K., Leone, V., Faraldo-Gómez, J. D., & Müller, V. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1115796109 · Cited by 131
Metadata
- Authors
- von Ballmoos, C., Wiedenmann, A., & Dimroth, P.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2009-06-01
- Volume
- 78
- Issue
- 1
- Pages
- 649-672
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2146941678
- Cited by
- 331
- References
- 82
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- closed
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- von Ballmoos, C., Wiedenmann, A., & Dimroth, P. (2009). Essentials for ATP Synthesis by F1F0 ATP Synthases. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.78.081307.104803
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.