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Bacteriol. 148, 30Ð42. COX, G. B., FIMMEL, A. L., GIBSON, F. AND HATCH, L. (1986). The mechanism of ATP synthase: A reassessment of the functions of the b and a subunits. Biochim. biophys. Acta 849, 62Ð69. DECKERS-HEBESTREIT, G., SIMONI, R. D. AND ALTENDORF, K. (1992). Influence of subunit-specific antibodies on the activity of the Fo complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies. J. biol. Chem. 267, 12364Ð12369. FILLINGAME, R. H. (1990). Molecular mechanics of ATP synthesis by F1Fo-type H+-transporting ATP synthases. In The Bacteria: A Treatise on Structure and Function, vol. XII (ed. T. A. Krulwich), pp. 345Ð391. New York: Academic Press. FILLINGAME, R. H., OLDENBURG, M. AND FRAGA, D.(1991). Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1Fo-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide. J. biol. Chem. 266, 20934Ð20939. FILLINGAME, R. H., PORTER, B., HERMOLIN, J. AND WHITE, L. K. (1986). Synthesis of a functional Fo sector of the Escherichia coli H+-ATPase does not require synthesis of the alpha or beta subunits of F1. J. Bacteriol. 165, 244Ð251. FRAGA, D. AND FILLINGAME, R. H. (1991). Essential residues in the polar loop region of subunit c of Escherichia coli F1Fo ATP synthase defined by random oligonucleotide-primed mutagenesis. J. Bacteriol. 173, 2639Ð2643. HENDERSON, R., BALDWIN, J. M., CESKA, T. A., ZEMLIN, F., BECKMANN, E. AND DOWNING, K. H.(1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. molec. Biol. 213, 899Ð929. HENSEL, M., DECKERS-HEBESTREIT, G., SCHMID, R. AND ALTENDORF, K. (1990). Orientation of subunit c of the ATP synthase of Escherichia coli Ð a study with peptide-specific antibodies. Biochim. biophys. Acta 1016, 63Ð70. HERMOLIN, J. AND FILLINGAME, R. H. (1989). H +-ATPase activity of Escherichia coli F1Fo is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the Fo complex. J. biol. Chem. 264, 3896Ð3903. HOPPE, J. AND SEBALD, W. (1986). Topological studies suggest that the pathway of the protons through Fo is provided by amino acid residues accessible from the lipid phase. Biochimie 68, 427Ð434. Fo complex of E. coli KAUFFER, S., DECKERS-HEBESTREIT, G. AND ALTENDORF, K. (1991). Substitution of the cysteinyl residue (Cys-21) of subunit b of the ATP synthase from Escherichia coli. Eur. J. Biochem. 202, 1307Ð1312. LAUBINGER, W. AND DIMROTH, P. (1988). Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump. Biochemistry, N.Y. 27, 7531Ð7537. LAUBINGER, W. AND DIMROTH, P. (1989). The sodium ion translocating ATPase of Propionigenium modestum pumps protons at low sodium ion concentrations. Biochemistry, N.Y. 28, 7194Ð7198. LEAR, J. D., WASSERMAN, Z. R. AND DEGRADO, W. F. (1988). Synthetic amphiphilic peptide models for protein ion channels. Science 240, 1177Ð1181. LEE, J. A., PUTTNER, I. B. AND KABACK, H. R. (1989). Effect of distance and orientation between arginine-302, histidine-322, and glutamate-325 on the activity of lac permease from Escherichia coli. Biochemistry, N.Y. 28, 2540Ð2544. LEWIS, M. J., CHANG, J. A. AND SIMONI, R. D. (1990). A topological analysis of subunit a from Escherichia coli F1Fo-ATP synthase predicts eight transmembrane segments. J. biol. Chem. 265, 10541Ð10550. LEWIS, M. J. AND SIMONI, R. D. (1992). Deletions in hydrophobic domains of subunit a from the Escherichia coli F1Fo-ATP synthase interfere with membrane insertion or Fo assembly. J. biol. Chem. 267, 3482Ð3489. LILL, H., ENGELBRECHT, S., SCHÖNKNECHT, G. AND JUNGE, W. (1986). The proton channel, CFo, in thylakoid membranes. Only a low proportion of CF1-lacking CFo is active with a high unit conductance (169 fS). Eur. J. Biochem. 160, 627Ð634. MILLER, M. J., OLDENBURG, M. AND FILLINGAME, R. H. (1990). The essential carboxyl group in subunit c of the F1Fo ATP synthase can be moved and H+-translocating function retained. Proc. natn. Acad. Sci. U.S.A. 87, 4900Ð4904. MORIYAMA, Y., IWAMOTO, A., HANADA, H., MAEDA, M. AND FUTAI, M. (1991). One-step purification of Escherichia coli H+-ATPase (FoF1) and its reconstitution into liposomes with neurotransmitter transporters. J. biol. Chem. 266, 22141Ð22146. NAGLE, J. F. AND TRISTAM-NAGLE, S. (1983). Hydrogen bonded chain mechanisms for proton conduction and proton pumping. J. Membr. Biol. 74, 1Ð14. NELSON, N.(1980). Proton channels in chloroplast membranes. Ann. N. Y. Acad. Sci. 358, 25Ð36. PATI, S. AND BRUSILOW, W. S. A.(1989). The roles of the a and g subunits in proton conduction through the Fo sector of the proton-translocating ATPase of Escherichia coli. J. biol. Chem. 264, 2640Ð2644. PATI, S., BRUSILOW, W. S. A., DECKERS-HEBESTREIT, G. AND ALTENDORF, K.(1991). Assembly of the Fo proton channel of the Escherichia coli F1Fo ATPase: Low conductance of reconstituted Fo sectors synthesized and assembled in the absence of F1. Biochemistry, N.Y. 30, 4711Ð4714. PORTER, A. C. G., KUMAMOTO, C., ALDAPE, K. AND SIMONI, R. D. (1985). Role of the b subunit of the Escherichia coli proton-translocating ATPase. A mutagenic analysis. J. biol. Chem. 260, 8182Ð8187. SCHNEIDER, E. AND ALTENDORF, K. (1984). Subunit b of the membrane moiety (Fo) of ATP synthase (F1Fo) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety. Proc. natn. Acad. Sci. U.S.A. 81, 7279Ð7283. SCHNEIDER, E. AND ALTENDORF, K. (1987). Bacterial adenosine 59-triphosphate synthase (F1Fo): Purification and reconstitution of Fo complexes and biochemical and functional characterization of their subunits. Microbiol. Rev. 51, 477Ð497. SCHÖNKNECHT, G., JUNGE, W., LILL, H. AND ENGELBRECHT, S. (1986). Complete tracking of proton flow in thylakoids Ð the unit conductance of CFo is greater than 10 fS. FEBS Lett. 203, 289Ð294. SENIOR, A. E. (1990). The proton-translocating ATPase of Escherichia coli. A. Rev. Biophys. biophys. Chem. 19, 7Ð41. STEFFENS, K., HOPPE, J. AND ALTENDORF, K. (1988). Fo part of the ATP synthase from Escherichia coli. Influence of subunits a and b on the structure of subunit c.Eur. J. Biochem. 170, 627Ð630. STEFFENS, K., SCHNEIDER, E., DECKERS-HEBESTREIT, G. AND ALTENDORF, K. (1987). Fo portion of Escherichia coli ATP synthase. Further resolution of trypsin-generated fragments of subunit b.J. biol. Chem. 262, 5866Ð5869. TAKEYAMA, M., NOUMI, T., MAEDA, M. AND FUTAI, M. (1988). Fo portion of Escherichia coli H+ATPase. Carboxyl-terminal region of the b subunit is essential for assembly of functional Fo. J. biol. Chem. 263, 16106Ð16112.

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