The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Structure, mechanism, and regulation of the chloroplast ATP synthase
Open accessAbstract
Protons find a path: Adenosine triphosphate (ATP) synthases are dynamos that interconvert rotational and chemical energy. Capturing the complete structure of these multisubunit membrane-bound complexes has been hindered by their inherent ability to adopt multiple conformations. Srivastava et al. used protein engineering to freeze mitochondrial ATP synthase from yeast in a single conformation and obtained a structure with the inhibitor oligomycin, which binds to the rotating c-ring within the membrane. Hahn et al. show that chloroplast ATP synthase contains a built-in inhibitor triggered by oxidizing conditions in the dark chloroplast. The mechanisms by which these machines are powered are remarkably similar: Protons are shuttled through a channel to the membrane-embedded c-ring, where they drive nearly a full rotation of the rotor before exiting through another channel on the opposite side of the membrane (see the Perspective by Kane). Science , this issue p. eaas9699 , p. eaat4318 ; see also p. 600
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Cited by
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Metadata
- Authors
- Hahn, A., Vonck, J., Mills, D. J., Meier, T., & Kühlbrandt, W.
- Venue
- Science
- Published
- 2018-05-11
- Volume
- 360
- Issue
- 6389
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2800754486
- Cited by
- 420
- References
- 68
- FWCI
- 13.50
- Type
- journal article
- Language
- en
- Open access
- green
- Funders
- Wellcome Trust (WT110068/Z/15/Z)
- Deutsche Forschungsgemeinschaft (CRC807)
- Max-Planck-Gesellschaft
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