H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function
暂无分享,去创建一个
[1] S. Dunn. The polar domain of the b subunit of Escherichia coli F1F0-ATPase forms an elongated dimer that interacts with the F1 sector. , 1992, The Journal of biological chemistry.
[2] R. D. Simoni,et al. Deletions in hydrophilic domains of subunit a from the Escherichia coli F1F0-ATP synthase interfere with membrane insertion or F0 assembly. , 1992, The Journal of biological chemistry.
[3] R. H. Fillingame,et al. Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide. , 1991, The Journal of biological chemistry.
[4] R. H. Fillingame,et al. Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis , 1991, Journal of bacteriology.
[5] R. E. Mccarty,et al. Subunit interactions within the chloroplast ATP synthase (CF0-CF1) as deduced by specific depletion of CF0 polypeptides. , 1990, The Journal of biological chemistry.
[6] R. H. Fillingame,et al. The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[7] R. D. Simoni,et al. A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments. , 1990, The Journal of biological chemistry.
[8] S. Howitt,et al. Mutational analysis of the function of the a-subunit of the F0F1-APPase of Escherichia coli. , 1990, Biochimica et biophysica acta.
[9] Christian Bjørbæk,et al. The transmembrane topology of the α subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions , 1990 .
[10] R. H. Fillingame. CHAPTER 12 – Molecular Mechanics of ATP Synthesis by F1F0-Type H+ -Transporting ATP Synthases , 1990 .
[11] R. H. Fillingame,et al. Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocation. , 1989, Archives of biochemistry and biophysics.
[12] P. Dimroth,et al. The sodium ion translocating adenosinetriphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations. , 1989, Biochemistry.
[13] M. Girvin,et al. Organization of the F0 sector of Escherichia coli H+-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane. , 1989, Biochemistry.
[14] R. H. Fillingame,et al. Conserved polar loop region of Escherichia coli subunit c of the F1F0 H+-ATPase. Glutamine 42 is not absolutely essential, but substitutions alter binding and coupling of F1 to F0. , 1989, The Journal of biological chemistry.
[15] R. H. Fillingame,et al. H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex. , 1989, The Journal of biological chemistry.
[16] B. Cain,et al. Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. , 1989, The Journal of biological chemistry.
[17] R. H. Fillingame,et al. Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0. , 1989, The Journal of biological chemistry.
[18] A. E. Senior,et al. ATP synthesis by oxidative phosphorylation. , 1988, Physiological reviews.
[19] S. Howitt,et al. The proton pore in the Escherichia coli F0F1-ATPase: a requirement for arginine at position 210 of the a-subunit. , 1987, Biochimica et biophysica acta.
[20] W. Sebald,et al. Topological studies suggest that the pathway of the protons through F0 is provided by amino acid residues accessible from the lipid phase. , 1986, Biochimie.
[21] R. H. Fillingame,et al. H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and Fo but not Fo-mediated H+ translocation. , 1985, The Journal of biological chemistry.
[22] J. Aris,et al. Cross-linking and labeling of the Escherichia coli F1F0-ATP synthase reveal a compact hydrophilic portion of F0 close to an F1 catalytic subunit. , 1983, The Journal of biological chemistry.
[23] R. H. Fillingame,et al. Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli. , 1982, The Journal of biological chemistry.
[24] R. L. Cross. The mechanism and regulation of ATP synthesis by F1-ATPases. , 1981, Annual review of biochemistry.
[25] R. H. Fillingame. The proton-translocating pumps of oxidative phosphorylation. , 1980, Annual review of biochemistry.