ATP synthase — a marvellous rotary engine of the cell
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/35089509.pdf
Reference76 articles.
1. Boyer, P. D. The ATP synthase — a splendid molecular machine. Annu. Rev. Biochem. 66, 717–749 (1997).Boyer's rotational catalysis and alternate-binding change model are concisely reviewed.
2. Mitchell, P. Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type mechanism. Nature 191, 144–148 (1961).This paper introduced a new concept of chemiosmotic theory into the field of bioenergetics.
3. Kanazawa, H., Kayano, T., Mabuchi, K. & Futai, M. Nucleotide sequence of the genes coding for α-, β- and γ-subunits of the proton-translocating ATPase of Escherichia coli. Biochem. Biophys. Res. Commun. 103, 604–612 (1981).
4. Walker, J. E., Fearnley, I. M., Gay, N. J., Gibson, B. W. & Tybulewicz, V. L. J. Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria. J. Mol. Biol. 184, 677–701 (1985).
5. Hudson, G. S. et al. A gene cluster in the spinach and pea chloroplast genomes encoding one CF1 and three CFo subunits of the H+-ATP synthase complex and the ribosomal protein S2. J. Mol. Biol. 196, 283–298 (1987).
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