Abstract
Structural changes in theEscherichia coli ATP synthase (ECF1F0) occur as part of catalysis, cooperativity and energy coupling within the complex. The γ and ε subunits, two major components of the stalk that links the F1 and F0 parts, are intimately involved in conformational coupling that links catalytic site events in the F1 part with proton pumping through the membrane embedded F0 sector. Movements of the γ subunit have been observed by electron microscopy, and by cross-linking and fluorescence studies in which reagents are bound to Cys residues introduced at selected sites by mutagenesis. Conformational changes and shifts of the ε subunit related to changes in nucleotide occupancy of catalytic sites have been followed by similar approaches.
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Capaldi, R.A., Aggeler, R., Wilkens, S. et al. Structural changes in the γ and ε subunits of theEscherichia coli F1F0-type ATPase during energy coupling. J Bioenerg Biomembr 28, 397–401 (1996). https://doi.org/10.1007/BF02113980
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DOI: https://doi.org/10.1007/BF02113980