Constant <i>c</i> ₁₀ Ring Stoichiometry in the <i>Escherichia coli</i> ATP Synthase Analyzed by Cross-Linking

Abstract

The subunit c stoichiometry of Escherichia coli ATP synthase was studied by intermolecular cross-linking via oxidation of bi-cysteine-substituted subunit c (cA21C/cM65C). Independent of the carbon source used for growth and independent of the presence of other FoF1 subunits, an equal pattern of cross-link formation stopping at the formation of decamers was obtained.