Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking.
J Bacteriol. 2009 Apr;191(7):2400-4. Epub 2009 Jan 30
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摘要
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.
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文献解读
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