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Journal of Bacteriology, April 2009, p. 2400-2404, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01390-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Constant c10 Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking{triangledown}

Britta Ballhausen, Karlheinz Altendorf, and Gabriele Deckers-Hebestreit*

Arbeitsgruppe Mikrobiologie, Fachbereich Biologie/Chemie, Universität Osnabrück, D-49069 Osnabrück, Germany

Received 3 October 2008/ Accepted 21 January 2009

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.

* Corresponding author. Mailing address: Arbeitsgruppe Mikrobiologie, Fachbereich Biologie/Chemie, Universität Osnabrück, D-49069 Osnabrück, Germany. Phone: 49 541 969 2809. Fax: 49 541 969 2870. E-mail: deckers-hebestreit{at}biologie.uni-osnabrueck.de

{triangledown} Published ahead of print on 30 January 2009.

Journal of Bacteriology, April 2009, p. 2400-2404, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01390-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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