The transmembrane domain of subunit b of the Escherichia coli F1FO ATP synthase is sufficient for H+-translocating activity together with subunits a and c
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.2004.04235.x/fullpdf
Reference33 articles.
1. Analysis of the nucleotide binding sites of mitochondrial ATP synthase provides evidence for a two-site catalytic mechanism;Berden;Biochim. Biophys. Acta,2000
2. ATP synthesis driven by proton transport in F1FO-ATP synthase;Weber;FEBS Lett.,2003
3. Structural model of the transmembrane FO rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ;Fillingame;Biochim. Biophys. Acta,2002
4. ATP synthase and other motor proteins;Junge;Proc. Natl Acad. Sci. USA,1999
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