ATP synthase synthesizes and hydrolyzes ATP by a unique rotational mechanism. A new study elucidates an important step of the catalytic mechanism, the timing of the release of the reaction product Pi in ATP hydrolysis.
This is a preview of subscription content, log in via an institution to check access.
References
Watanabe, R., Iino, R. & Noji, H. Nat. Chem. Biol. 6, 814–820 (2010).
Nishizaka, T. et al. Nat. Struct. Mol. Biol. 11, 142–148 (2004).
Shimo-Kon, R. et al. Biophys. J. 98, 1227–1236 (2010).
Weber, J., Wilke-Mounts, S., Lee, R.S., Grell, E. & Senior, A.E. J. Biol. Chem. 268, 20126–20133 (1993).
Mao, H.Z. & Weber, J. Proc. Natl. Acad. Sci. U.S.A. 104, 18478–18483 (2007).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Competing interests
The author declares no competing financial interests.
Rights and permissions
About this article
Cite this article
Weber, J. Toward the ATP synthase mechanism. Nat Chem Biol 6, 794–795 (2010). https://doi.org/10.1038/nchembio.458
Published:
Issue Date:
DOI: https://doi.org/10.1038/nchembio.458
- Springer Nature America, Inc.
This article is cited by
-
Engineering of stimuli-responsive lipid-bilayer membranes using supramolecular systems
Nature Reviews Chemistry (2020)
-
ATP hydrolysis assists phosphate release and promotes reaction ordering in F1-ATPase
Nature Communications (2015)
-
Timing of inorganic phosphate release modulates the catalytic activity of ATP-driven rotary motor protein
Nature Communications (2014)
-
Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation
Scientific Reports (2014)
-
Arrayed lipid bilayer chambers allow single-molecule analysis of membrane transporter activity
Nature Communications (2014)