The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
ATP Synthase
Open accessAbstract
Oxygenic photosynthesis is the principal converter of sunlight into chemical energy. Cyanobacteria and plants provide aerobic life with oxygen, food, fuel, fibers, and platform chemicals. Four multisubunit membrane proteins are involved: photosystem I (PSI), photosystem II (PSII), cytochrome b 6 f (cyt b 6 f), and ATP synthase (F O F 1). ATP synthase is likewise a key enzyme of cell respiration. Over three billion years, the basic machinery of oxygenic photosynthesis and respiration has been perfected to minimize wasteful reactions. The proton-driven ATP synthase is embedded in a proton tight-coupling membrane. It is composed of two rotary motors/generators, F O and F 1, which do not slip against each other. The proton-driven F O and the ATP-synthesizing F 1 are coupled via elastic torque transmission. Elastic transmission decouples the two motors in kinetic detail but keeps them perfectly coupled in thermodynamic equilibrium and (time-averaged) under steady turnover. Elastic transmission enables operation with different gear ratios in different organisms.
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Cites
Comparing Photosynthetic and Photovoltaic Efficiencies and Recognizing the Potential for Improvement
Blankenship, R. E., Tiede, D. M., Barber, J., Brudvig, G. W., Fleming, G., Ghirardi, M., Gunner, M. R., Junge, W., Kramer, D. M., Melis, A., et al. (2011) · Science · doi:10.1126/science.1200165 · Cited by 1,638
Self-citationThe ATP synthase: the understood, the uncertain and the unknown
Walker, J. E. (2013) · Biochemical Society Transactions · doi:10.1042/bst20110773 · Cited by 614
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
Cited by
Mechanically Interlocked Molecules (MIMs)—Molecular Shuttles, Switches, and Machines (Nobel Lecture)
Stoddart, J. F. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201703216 · Cited by 1,041
Emerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Mesa-Galloso, H., Abdizadeh, H., Noskov, S. Y., Marrink, S. J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 459
Osmosis, from molecular insights to large-scale applications
Marbach, S., & Bocquet, L. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00420j · Cited by 316
Building machines with DNA molecules
Ramezani, H., & Dietz, H. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-019-0175-6 · Cited by 284
Islam, W., Adnan, M., Shabbir, A., Naveed, H., Abubakar, Y. S., Qasim, M., Tayyab, M., Noman, A., Nisar, M. S., Khan, K. A., et al. (2021) · Microbial Pathogenesis · doi:10.1016/j.micpath.2021.105122 · Cited by 259
Metadata
- Authors
- Junge, W., & Nelson, N.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2015-06-02
- Volume
- 84
- Issue
- 1
- Pages
- 631-657
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W4254804607
- Cited by
- 351
- References
- 3
- FWCI
- 2.14
- Type
- journal article
- Language
- en
- Open access
- bronze
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