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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP Synthetase Complexes / chemistry*
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ATP Synthetase Complexes / genetics
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ATP Synthetase Complexes / metabolism
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Bacterial Proton-Translocating ATPases / chemistry*
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Bacterial Proton-Translocating ATPases / genetics
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Bacterial Proton-Translocating ATPases / metabolism
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Cross-Linking Reagents / chemistry
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Escherichia coli / chemistry*
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism
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Oxidation-Reduction
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Protein Subunits / chemistry
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Protein Subunits / genetics
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Protein Subunits / metabolism
Substances
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Cross-Linking Reagents
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Escherichia coli Proteins
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Protein Subunits
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ATP Synthetase Complexes
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ATP synthase subunit c, E coli
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Bacterial Proton-Translocating ATPases