ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the γ subunit relative to the β subunits

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1275, Issue 1-2, 1996, Pages 96-100

  Zhou, Yuantai ^a   Duncan, Thomas M ^a   Bulygin, Vladimir V ^a   Hutcheon, Marcus L ^a   Cross, Richard L ^a  

^a SUNY UPSTATE MEDICAL UNIVERSITY   (United States)

Author keywords

ATP hydrolysis; Binding change mechanism; H+ transporting ATP synthase; Membrane; Physiological relevance; Subunit rotation

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; MEMBRANE BINDING; PRIORITY JOURNAL;

EID: 0030592156     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/0005-2728(96)00056-4     Document Type: Conference Paper

References (23)

1. [1] Penefsky, H.S. and Cross, R.L. (1991) in Advances in Enzymology and Related Areas of Molecular Biology (Meister, A., ed.), Vol. 64, pp. 173-214.
2. [2] Cox, G.B., Devenish, R.J., Gibson, F., Howitt, S.M. and Nagley, P. (1992) in Molecular Mechanisms in Bioenergetics (Ernster, L., ed.), pp. 283-315.
3. [3] Capaldi, R.A., Aggeler, R., Turina, P. and Wilkens, S. (1994) Trends Biochem. Sci. 19, 284-289.
4. [4] Abrahams, J.P., Leslie, A.G., Lutter, R. and Walker, J.E. (1994) Nature 370, 621-628.
5. [5] Boyer, P.D. (1993) Biochim. Biophys. Acta 1140, 215-250.
6. [6] Boyer, P.D., Cross, R.L. and Momsen, W. (1973) Proc. Natl. Acad. Sci. USA 70, 2837-2839.
7. [7] Kayalar, C., Rosing, J. and Boyer, P.D. (17) J. Biol. Chem. 252, 2486-2491.
8. [8] Boyer, P.D. and Kohlbrenner, W.E. (1981) in Energy Coupling in Photosythesis (Selman, B. and Selman-Reiner, S., eds.), pp. 231-240, Elsevier-North Holland, New York.
9. [9] Duncan, T.M., Zhou, Y., Bulygin, V., Hutcheon, M.L. and Cross, R.L. (1995) Biochem. Soc. Trans. 23, 736-741.
10. [10] Duncan, T.M., Bulygin, V.V., Zhou, Y., Hutcheon, M.L. and Cross, R.L. (1995) Proc. Natl. Acad. Sci. USA 92, 10964-10968.
11. [11] Hopp, T.P., Prickett, K.S., Price, V., Libby, R.T., March, C.J., Cerretti, P., Urdal, D.L. and Conlon, P.J. (1988) Biotech. 6, 1205-1210.
12. [12] Prickelt, K.S., Amberg, D.C. and Hopp, T.P. (1989) Biotech. 7, 580-589.
13. [13] Brizzard, B.L., Chubet, R.G. and Vizard, D.L. (1994) Biotech. 16, 730-735.
14. [14] Landt, O., Grunert, H.-P. and Hahn, U. (1990) Gene 96, 125-128.
15. [15] Walker, J.E., Auffret, A.D., Carne, A., Gurnett, A., Hanisch, P., Hill, D. and Saraste, M. (1982) Eur. J. Biochem. 123, 253-260.
16. [16] Tozer, R.G. and Dunn, S.D. (1986) Eur. J. Biochem. 161, 513-518.
17. [17] Ziegler, M., Xiao, R. and Penefsky, H.S. (1994) J. Biol. Chem. 269, 4233-4239.
18. [18] Lee, R.S., Pagan, J., Wilke-Mounts, S. and Senior, A.E. (1991) Biochemistry 30, 6842-6847.
19. [19] Senior, A.E., Fayle, D.R.H., Downie J.A., Gibson, F. and Cox, G.B. (1979) Biochem. J. 180, 111-118.
20. [20] Perlin, D.S., Cox, D.N. and Senior, A.E. (1983) J. Biol. Chem. 258, 9793-9800.
21. [21] Penefsky, H.S. (1977) J. Biol. Chem. 252, 2891-2899.
22. [22] Penefsky, H.S. (1985) Proc. Natl. Acad. Sci. USA 82, 1589-1593.
23. [23] Matsuno-Yagi, A., Tahi, T. and Hatefi, Y. (1985) Proc. Natl. Acad. Sci. USA 82, 7550-7554