| Literature DB >> 19181809 |
Britta Ballhausen1, Karlheinz Altendorf, Gabriele Deckers-Hebestreit.
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.Entities:
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Year: 2009 PMID: 19181809 PMCID: PMC2655506 DOI: 10.1128/JB.01390-08
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490