Δψ and ΔpH are equivalent driving forces for proton transport through isolated F0 complexes of ATP synthases

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1777, Issue 10, 2008, Pages 1301-1310

  Wiedenmann, Alexander ^a   Dimroth, Peter ^a   von Ballmoos, Christoph ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

ATP synthase; Driving force; F0 part; H+ transport; Pyranine

Indexed keywords

HOLOENZYME; LIPOSOME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; IONOPHORE; ORGANOTIN COMPOUND; PROTON; TRIBUTYLTIN; VALINOMYCIN;

ACCURACY; ARTICLE; CATALYSIS; ESCHERICHIA COLI; FLUORESCENCE; HYDROLYSIS; IN VITRO STUDY; KINETICS; MATHEMATICAL ANALYSIS; MEMBRANE POTENTIAL; NONHUMAN; PH; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTON TRANSPORT; SIGNAL NOISE RATIO; SYNTHESIS; CHEMISTRY; CHLOROPLAST; CYTOLOGY; ENZYMOLOGY; ION TRANSPORT; METABOLISM; MITOCHONDRIAL MEMBRANE POTENTIAL; PHYSIOLOGY; PROTON MOTIVE FORCE; SPINACH;

ESCHERICHIA COLI;

CHLOROPLASTS; ESCHERICHIA COLI; ION TRANSPORT; IONOPHORES; LIPOSOMES; MEMBRANE POTENTIAL, MITOCHONDRIAL; MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES; PROTON-MOTIVE FORCE; PROTONS; SPINACIA OLERACEA; TRIALKYLTIN COMPOUNDS; VALINOMYCIN;

EID: 52949102534     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.06.008     Document Type: Article

References (25)

1. Boyer P.D. The ATP synthase- a splendid molecular machine. Annu. Rev. Biochem. 66 (1997) 717-749
2. Meier T., Morgner N., Matthies D., Pogoryelov D., Keis S., Cook G.M., Dimroth P., and Brutschy B. A tridecameric c ring of the adenosine triphosphate (ATP) synthase from the thermoalkaliphilic Bacillus sp. strain TA2.A1 facilitates ATP synthesis at low electrochemical proton potential. Mol. Microbiol. 65 (2007) 1181-1192
3. +-ATPases from Escherichia coli or chloroplasts reconstituted into liposomes. FEBS Lett. 457 (1999) 327-332
4. 1) and its reconstitution into liposomes with neurotransmitter transporters. J. Biol. Chem. 266 (1991) 22141-22146
5. Klionsky D.J., Brusilow W.S., and Simoni R.D. In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160 (1984) 1055-1060
6. 0 ATP synthase. Biochim. Biophys. Acta 1706 (2005) 110-116
7. 1-liposomes. EMBO J. 22 (2003) 418-426
8. Senior A.E., Downie J.A., Cox G.B., Gibson F., Langman L., and Fayle D.R. The uncA gene codes for the alpha-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains. Biochem. J. 180 (1979) 103-109
9. Laubinger W., and Dimroth P. Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump. Biochemistry 27 (1988) 7531-7537
10. Brune A., Spillecke J., and Kroger A. Correlation of the turnover number of the ATP synthase in liposomes with the proton flux and the proton potential across the membrane. Biochim. Biophys. Acta 893 (1987) 499-507
11. 0 sectors from Escherichia coli. Biophys. J. 87 (2004) 3594-3599
12. 0 complex of the Escherichia coli ATP synthase. Investigation by electron spectroscopic imaging and immunoelectron microscopy. Eur. J. Biochem. 230 (1995) 58-67
13. Dencher N.A., Burghaus P.A., and Grzesiek S. Determination of the net proton-hydroxide ion permeability across vesicular lipid bilayers and membrane proteins by optical probes. Methods Enzymol. 127 (1986) 746-760
14. Kriz J., Makrlik E., and Vanura P. NMR evidence of a valinomycin-proton complex. Biopolymers 81 (2006) 104-109
15. 1 ATP synthase for ATP synthesis in membrane vesicles. Eur. J. Biochem. 243 (1997) 336-343
16. 1) and effects of tyrosyl residue modification. J. Biol. Chem. 256 (1981) 2873-2877
17. o. Cell Biochem. Biophys. 34 (2001) 305-320
18. 0 is active with a high unit conductance (169 fS). Eur. J. Biochem. 160 (1986) 627-634
19. Feniouk B.A., Kozlova M.A., Knorre D.A., Cherepanov D.A., Mulkidjanian A.Y., and Junge W. The proton-driven rotor of ATP synthase: ohmic conductance (10 fS), and absence of voltage gating. Biophys. J. 86 (2004) 4094-4109
20. Greie J.C., Deckers-Hebestreit G., and Altendorf K. Secondary structure composition of reconstituted subunit b of the Escherichia coli ATP synthase. Eur. J. Biochem. 267 (2000) 3040-3048
21. Hoppe J., Schairer H.U., Friedl P., and Sebald W. An Asp-Asn substitution in the proteolipid subunit of the ATP-synthase from Escherichia coli leads to a non-functional proton channel. FEBS Lett. 145 (1982) 21-29
22. 1-ATP synthases of chloroplasts and Escherichia coli with special emphasis on subunit delta. Eur. J. Biochem. 181 (1989) 485-491
23. 0 ATPase from Propionigenium modestum: discovery of a membrane potential dependent step. Biochemistry 31 (1992) 12665-12672
24. von Ballmoos C., Brunner J., and Dimroth P. The ion channel of F-ATP synthase is the target of toxic organotin compounds. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 11239-11244
25. Selwyn M.J., Dawson A.P., Stockdale M., and Gains N. Chloride-hydroxide exchange across mitochondrial, erythrocyte and artificial lipid membranes mediated by trialkyl- and triphenyltin compounds. Eur. J. Biochem. 14 (1970) 120-126