H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function
- 1 October 1992
- journal article
- review article
- Published by Springer Nature in Journal of Bioenergetics and Biomembranes
- Vol. 24 (5) , 485-491
- https://doi.org/10.1007/bf00762366
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained.Proceedings of the National Academy of Sciences, 1990
- Mutational analysis of the function of the a-subunit of the F0F1-ATPase of Escherichia coliBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1990
- The transmembrane topology of the α subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusionsFEBS Letters, 1990
- Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocationArchives of Biochemistry and Biophysics, 1989
- The sodium ion translocating adenosine triphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrationsBiochemistry, 1989
- Organization of the F0 sector of Escherichia coli proton-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membraneBiochemistry, 1989
- The proton pore in the Escherichia coli F0F1-ATPase: A requirement for arginine at position 210 of the a-subunitBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1987
- Topological studies suggest that the pathway of the protons through F0 is provided by amino acid residues accessible from the lipid phaseBiochimie, 1986
- The Mechanism and Regulation of ATP Synthesis by F1-ATPasesAnnual Review of Biochemistry, 1981
- The Proton-Translocating Pumps of Oxidative PhosphorylationAnnual Review of Biochemistry, 1980