Constant c 10 Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking
Author:
Affiliation:
1. Arbeitsgruppe Mikrobiologie, Fachbereich Biologie/Chemie, Universität Osnabrück, D-49069 Osnabrück, Germany
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JB.01390-08
Reference33 articles.
1. Arechaga, I., P. J. G. Butler, and J. E. Walker. 2002. Self-assembly of ATP synthase subunit c rings. FEBS Lett. 515 : 189-193.
2. Birkenhäger, R., J.- C. Greie, K. Altendorf, and G. Deckers-Hebestreit. 1999. Fo complex of the Escherichia coli ATP synthase. Not all monomers of the subunit c oligomer are involved in F1 interaction. Eur. J. Biochem. 264 : 385-396.
3. atp Mutants of Escherichia coli Fail To Grow on Succinate Due to a Transport Deficiency
4. Dimroth, P., C. von Ballmoos, and T. Meier. 2006. Catalytic and mechanical cycles in F-ATP synthases. EMBO Rep. 7 : 276-282.
5. Dmitriev, O. Y., P. C. Jones, and R. H. Fillingame. 1999. Structure of the subunit c oligomer of the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme. Proc. Natl. Acad. Sci. USA 96 : 7785-7790.
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