Journal
JOURNAL OF BACTERIOLOGY
Volume 191, Issue 7, Pages 2400-2404Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.01390-08
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- Deutsche Forschungsgemeinschaft [SFB 431/P2]
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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 F0F1 subunits, an equal pattern of cross-link formation stopping at the formation of decamers was obtained.
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