The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Proton-powered turbine of a plant motor
Open accessAbstract
ATP synthases are enzymes that can work in two directions to catalyse either the synthesis or breakdown of ATP, and they constitute the smallest rotary motors in biology. The flow of protons propels the rotation of a membrane-spanning complex of identical protein subunits, the number of which determines the efficiency of energy conversion. This proton-powered turbine is predicted to consist of 12 subunits, based on data for Escherichia coli. The yeast mitochondrial enzyme, however, has only 10 subunits. We have imaged the ATP synthase from leaf chloroplasts by using atomic force microscopy and, surprisingly, find that its turbine has 14 subunits, arranged in a cylindrical ring.
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Citations
Cites
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
Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F 0 F 1 ): Direct Observation
Sambongi, Y., Iko, Y., Tanabe, M., Omote, H., Iwamoto-Kihara, A., Ueda, I., Yanagida, T., Wada, Y., & Futai, M. (1999) · Science · doi:10.1126/science.286.5445.1722 · Cited by 446
Structural changes linked to proton translocation by subunit c of the ATP synthase
Rastogi, V. K., & Girvin, M. E. (1999) · Nature · doi:10.1038/46224 · Cited by 443
Electrostatically Balanced Subnanometer Imaging of Biological Specimens by Atomic Force Microscope
Müller, D. J., Fotiadis, D., Scheuring, S., Müller, S. A., & Engel, A. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77275-9 · Cited by 354
Self-citationTransient accumulation of elastic energy in proton translocating ATP synthase
Cherepanov, D. A., Mulkidjanian, A. Y., & Junge, W. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00386-5 · Cited by 153
Genetic Fusions of Subunit c in the F0Sector of H+-transporting ATP Synthase
Jones, P. C., & Fillingame, R. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29701 · Cited by 112
ATP synthase and other motor proteins
Junge, W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4735 · Cited by 98
Schemidt, R. A., Qu, J., Williams, J. R., & Brusilow, W. S. A. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.12.3205-3208.1998 · Cited by 88
Cited by
ATP synthase — a marvellous rotary engine of the cell
Yoshida, M., Muneyuki, E., & Hisabori, T. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35089509 · Cited by 956
The complex architecture of oxygenic photosynthesis
Nelson, N., & Ben-Shem, A. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1525 · Cited by 709
The Importance of Energy Balance in Improving Photosynthetic Productivity
Kramer, D. M., & Evans, J. R. (2011) · Plant Physiology · doi:10.1104/pp.110.166652 · Cited by 494
Probing Liquid/Solid Interfaces at the Molecular Level
Zaera, F. (2012) · Chemical Reviews · doi:10.1021/cr2002068 · Cited by 458
Determining the limitations and regulation of photosynthetic energy transduction in leaves
BAKER, N. R., HARBINSON, J., & KRAMER, D. M. (2007) · Plant, Cell & Environment · doi:10.1111/j.1365-3040.2007.01680.x · Cited by 454
Metadata
- Authors
- Seelert, H., Poetsch, A., Dencher, N. A., Engel, A., Stahlberg, H., & Müller, D. J.
- Venue
- Nature
- Published
- 2000-05
- Volume
- 405
- Issue
- 6785
- Pages
- 418-419
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1591326119
- Cited by
- 465
- References
- 8
- FWCI
- 11.94
- Type
- journal article
- Language
- en
- Open access
- green
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- Seelert, H., Poetsch, A., Dencher, N. A., Engel, A., Stahlberg, H., & Müller, D. J. (2000). Proton-powered turbine of a plant motor. Nature. https://doi.org/10.1038/35013148
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.