Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking.
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.
Ballhausen
Britta
B
Arbeitsgruppe Mikrobiologie, Fachbereich Biologie/Chemie, Universität Osnabrück, Germany.
Altendorf
Karlheinz
K
Deckers-Hebestreit
Gabriele
G
D025181:ATP Synthetase Complexes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry* / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010084:Oxidation-Reduction; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D003432:Cross-Linking Reagents; D029968:Escherichia coli Proteins; D021122:Protein Subunits; D025181:ATP Synthetase Complexes; C523987:ATP synthase subunit c, E coli; D025243:Bacterial Proton-Translocating ATPases