Energy transduction in the F1 motor of ATP synthase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/24409.pdf
Reference19 articles.
1. Abrahams, J., Leslie, A., Lutter, R. & Walker, J. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621–628 (1994).
2. Boyer, P. The binding change mechanism for ATP synthase—some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215–250 (1993).
3. Fillingame, R. H. Coupling H+ transport and ATP synthesis in F1Fo-ATP synthases: glimpses of interacting parts in a dynamic molecular machine. J. Exp. Biol. 200, 217–224 (1997).
4. Cross, R. & Duncan, T. Subunit rotation in FoF1-ATP synthases as a means of coupling proton transport through Foto the binding changes in F1. J. Bioen. Biomembr. 28, 403–408 (1996).
5. Noji, H., Yasuda, R., Yoshida, M. & Kinosita, K. Direct observation of the rotation of F1-ATPase. Nature 386, 299–302 (1997).
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