ATP synthase research has reached a milestone as single-molecule techniques are used to examine the direction and stepping of the proton gradient–driven rotation, to determine the effect of forced rotation on ATP synthesis and to synchronously monitor rotation and nucleotide kinetics.
References
Noji, H., Yasuda, R., Yoshida, M. & Kinosita, K. Nature 386, 299–302 (1997).
Diez, M. et al. Nat. Struct. Mol. Biol. 11, 135–141 (2004).
Itoh, H. et al. Mechanically-driven ATP synthesis by F1-ATPase. Nature in the press (2004).
Nishizaka, T. et al. Nat. Struct. Mol. Biol. 142–148 (2004).
Weber, J. & Senior, A.E. FEBS Lett. 545, 61–70 (2003).
Noji, H. & Yoshida, M. J. Biol. Chem. 276, 1665–1668 (2001).
Weber, J. & Senior, A.E. Biochim. Biophys. Acta 1458, 300–309 (2000).
Leslie, A.G.W. & Walker, J.E. Phil. Trans. R. Soc. Lond. B 355, 465–472 (2000).
Acknowledgements
A.E.S. gratefully acknowledges support from US National Institutes of Health grant GM25349.
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Senior, A., Weber, J. Happy motoring with ATP synthase. Nat Struct Mol Biol 11, 110–112 (2004). https://doi.org/10.1038/nsmb0204-110
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DOI: https://doi.org/10.1038/nsmb0204-110
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