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Insights into ATP Synthase Structure and Function Using Affinity and Site-Specific Spin Labeling

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Abstract

A variety of different approaches has been used during the last couple of decades to investigatestructure and function relationships within the catalytic portion of the F0F1-ATP synthase andof its interactions with the proton-translocator F0. In our group, we employ ESR spectroscopywith the use of stable organic radicals, so-called spin labels, as reporter groups. The radicalsare either attached to substrates/ligands or specifically inserted into the protein structure by“site-specific spin labeling.” Both approaches bear intrinsic advantages for their special usesand result in the specific information that is available through ESR, e.g., structural changesdue to binding of effector molecules (e.g., Mg2+ ions), conformational transitions duringcatalytic turnover, distance information on radicals bound at 20 Å or less, and information onthe binding characteristics of labeled substrates. This review summarizes the results of a varietyof different approaches we have used during the last years to study, with the help of ESRspectroscopy, the structure of the nucleotide binding sites of F1-ATPases of different originsas well as interactions with F0 subunits.

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REFERENCES

  • Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994). Nature (London) 370, 621–628.

    Google Scholar 

  • Bianchet, M. A., Hullihen, J., Pedersen, P. L., and Amzel, L. M. (1998). Proc. Natl. Acad. Sci. USA 95, 11065–11070.

    Google Scholar 

  • Boos, K. S., Lüstorff, J., Schlimme, E., Hesse, H., and Strotmann, H. (1976). FEBS Lett. 71, 124–129.

    Google Scholar 

  • Boyer, P. D. (1993). Biochim. Biophys. Acta 1140, 215–250.

    Google Scholar 

  • Boyer, P. D., Cross, R. L., and Moonsen, W. (1973). Proc. Natl. Acord. Sci. USA 70, 2837–2839.

    Google Scholar 

  • Bullough, D. A. and Allison, W. S. (1988). Biochim. Biophys. Acta 934, 397–400.

    Google Scholar 

  • Burgard, S., Nett, J. H., Kagawa, Y., Schäfer, H.-J., Wise, J. G., Vogel, P. D., and Trommer, W. E. (1994). J. Biol. Chem. 269, 17815–17819.

    Google Scholar 

  • Cross, R. L. (1981). Annu. Rev. Biochem. 50, 681–714.

    Google Scholar 

  • Cross, R. L. and Nalin, C. M. (1982). J. Biol. Chem. 257, 2874–2881.

    Google Scholar 

  • Cross, R. L., Cunningham, D., Miller, C. G., Xue, Z., Zhou, J.-M., and Boyer, P. D.(1987). Proc. Natl. Acad. Sci. USA 84, 5715–5719.

    Google Scholar 

  • Damerau, W. and Fittkau, S. (1983). Stud. Biophys. 96, 177–186.

    Google Scholar 

  • Dann, M. D. and McCarty, R. E. (1992). Plant Physiol. 99, 153–160.

    Google Scholar 

  • Di Pietro, A., Penin, F., Godinot, C., and Gautheron, D. C. (1980). Biochemistry 19, 5671–5678.

    Google Scholar 

  • Divita, G., Goody, R. S., Gautheron, D., and Di Pietro, A. (1993). J. Biol. Chem. 268, 13178–13186.

    Google Scholar 

  • Duncan, T. M., Bulygin, V.V., Zhou, Y., Hutcheon, M. L., and Cross, R. L. (1995). Proc. Natl. Acad. Sci. USA 92, 10964–10968.

    Google Scholar 

  • Dunn, S. D. (1992). J. Biol. Chem. 267, 7630–7636.

    Google Scholar 

  • Dunn, S. D., McLachlin, D. T., and Revington, M. (2000). Biochim Biophys. Acta 1458, 356–363.

    Google Scholar 

  • Erbse, A. H., Burgard, S., Harada, M., Kagawa, Y., Trommer W. E., and Vogel, P. D., (1996) unpublished results.

  • Feix, J. B. and Klug, C. S. (1998) in Biological Magnetic Resonance, Spin Labeling, The Next Millenium, Vol. 14 (Berliner, L. J., ed.), Plenum Press, New York, pp. 251–279.

    Google Scholar 

  • Garin, J., Boulay, F., Issartel, J. P., Lunardi, J., and Vignais, P. V. (1986). Biochemistry 25, 4431–4437.

    Google Scholar 

  • Garin, J., Vignais, P. V., Gronenborn, A. M., Clore, G. M., Gao, Z., and Ba¨uerlein, E. (1988). FEBS Lett. 242, 178–182.

    Google Scholar 

  • Guerrero, K. J. and Boyer, P. D. (1989). Biochem. Biophys. Res. Commun. 154, 854–860.

    Google Scholar 

  • Haller, M., Hoffmann, U., Schanding, T., Goody, R. S., and Vogel, P. D. (1997). J. Biol. Chem. 272, 30103–30107.

    Google Scholar 

  • Harada, M., Ito, Y., Sato, M., Aono, O., Ohta, S., and Kagawa, Y. (1991). J. Biol. Chem. 266, 11455–11460.

    Google Scholar 

  • Hartmann, D., Philipp, R., Schmadel, K., Birktoft, J. J., Banaszak, L. J., and Trommer, W. E. (1991). Biochemistry 30, 2782–2790.

    Google Scholar 

  • Karim, C., Philipp, R., Trommer, W. E., and Park, J. (1989). Biol. Chem. Hoppe-Seyler 370, 1245–1252.

    Google Scholar 

  • Kersten, M. V., Dunn, S. D., Wise, J. G., and Vogel, P. D. (2000). Biochemistry 39, 3856–3860.

    Google Scholar 

  • Kinosita, K., Jr., Yasuda, R., Noji, H., and Adachi, K. (2000). Phil. Trans. R. Soc. Lond. B Biol. Sci. 473–489.

  • Kraft, G., Kersten, M. V., Motz, C., Hornung, T., Wise, J. G., and Vogel, P. D., (1999) unpublished.

  • Kuo, P. H., Ketchum, C. J., and Nakamoto, R. K. (1998). FEBS Lett. 426, 217–220.

    Google Scholar 

  • Lien, S. and Racker, E. (1971). Methods Enzymol. 23, 547–555.

    Google Scholar 

  • Lösel, R. M., Erbse, A. H., Nett, J. H., Wise, J. G., Berger, G., Girault, G., and Vogel, P. D. (1996). Spectrochim. Acta Part A 52, 73–83.

    Google Scholar 

  • Lösel, R. M., Wise, J. G., and Vogel, P. D. (1997). Biochemistry 35, 1188–1193.

    Google Scholar 

  • McConnell, H. M. and McFarland, B. G. (1970). Quart. Rev. Biophys. 3, 91–136.

    Google Scholar 

  • McLachlin, D. T. and Dunn, S. D. (1997). J. Biol. Chem. 272, 21233–21239.

    Google Scholar 

  • McLachlin, D. T., Coveny, A. M., Clark, S. M., and Dunn, S. D. (2000). J. Biol. Chem. 275, 17571–17577.

    Google Scholar 

  • Milgrom, Y. M., Ehler, L. L., and Boyer, P. D. (1990). J. Biol. Chem. 265, 18725–18728.

    Google Scholar 

  • Milgrom, Y. M., Ehler, L. L., and Boyer, P. D. (1991). J. Biol. Chem. 266, 11551–11558.

    Google Scholar 

  • Motz, C., Wise, J. G., and Vogel, P. D., (1999) unpublished results.

  • Neuhofen, S., Theyssen, H., Reinstein, J., Trommer, W. E., and Vogel, P. D. (1996). Eur. J. Biochem. 240, 78–82.

    Google Scholar 

  • Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K., Jr. (1997). Nature (London) 386, 299–302.

    Google Scholar 

  • Park, J. H. and Trommer, W. E. (1989) in Biological Magnetic Resonance,Vol. 8 (Berliner, L. J., and Reuben, J., eds.) Plenum, New York, pp. 547–595.

    Google Scholar 

  • Penefsky, H. S. (1977). J. Biol. Chem. 252, 2891–2899.

    Google Scholar 

  • Rabenstein, M. D. and Shin, Y. K. (1995). Proc. Natl. Acad. Sci. USA 92, 8239–8243.

    Google Scholar 

  • Sabbert, D., Engelbrecht, S., and Junge W. (1996). Nature (London) 381, 623–625.

    Google Scholar 

  • Scheibel, T., Neuhofen, S., Weikl, T., Mayr, C., Reinstein, J., Vogel, P. D., and Buchner, J. (1997). J. Biol. Chem. 272, 18608–18613.

    Google Scholar 

  • Shirakihara, Y., Leslie, A. G., Abrahams, J. P., Walker, J. E., Ueda, T., Sekimoto, Y., Kambara, M., Saika, K., Kagawa, Y., and Yoshida, M. (1997). Structure 5, 825–836.

    Google Scholar 

  • Stock, D., Leslie, A. G., and Walker, J. E. (1999). Science 286, 1700–1705.

    Google Scholar 

  • Streckenbach, B., Schwarz, D., and Repke, K. H. R. (1980). Biochim. Biophys. Acta 601, 34–46.

    Google Scholar 

  • Trommer, W. E. (1987). in Pyridine Nucleotide Coenzymes: Chemical, Biochemical, and Medical Aspects, Vol. 29 (Dolphin, D. et al., eds.), J Wiley, New York, pp. 613–639.

    Google Scholar 

  • Trommer, W. E. and Vogel, P. D. (1992). in Bioactive Spin Labels (Zhdanov, R. I., ed.), Springer Verlag, Berlin, Heidelberg, pp. 405–428.

    Google Scholar 

  • Vogel, P. D., Nett, J. H., Sauer, H. E., Schmadel, K., Cross, R. L., and Trommer, W. E. (1992). J. Biol. Chem. 267, 11982–11986.

    Google Scholar 

  • Vogel-Claude, P., Scha¨fer, G., and Trommer, W. E. (1988). FEBS Lett. 227, 107–109.

    Google Scholar 

  • Volodarsky, L. B. (1988). Imidazoline Nitroxides, Vol. 1, CRC Press, Boca Raton, Florida.

    Google Scholar 

  • Weber J., Wilke-Mounts, S., Grell, E., and Senior, A. E. (1994). J. Biol. Chem. 269, 11261–11268.

    Google Scholar 

  • Wilder, R. T., Venkataramu, S. D., Dalton, L. R., Birktoft, J. J., Trommer, W. E., and Park, J. H. (1989). Biochim. Biophys. Acta 997, 65–77.

    Google Scholar 

  • Wise, J. G. (1990). J. Biol. Chem. 265, 10403–10409.

    Google Scholar 

  • Wise, J. G. and Senior, A. E. (1985). Biochemistry 24, 6949–6954.

    Google Scholar 

  • Wise, J. G. Duncan, T. M., Latchney, L. R., Cox, D. N., and Senior, A.E. (1983). Biochem. J. 215, 343–350.

    Google Scholar 

  • Wise, J. G., Hicke, B. J., and Boyer, P. D. (1987). FEBS Lett. 223, 395–401.

    Google Scholar 

  • Xue, Z., Miller, C. G., Zhou, J.-M., and Boyer, P. D. (1987). FEBS Lett. 223, 391–394.

    Google Scholar 

  • Xue, Z., Zhou, J.-M., Melese, T., Cross, R. L., and Boyer, P. D. (1987a). Biochemistry 26, 3749–3753.

    Google Scholar 

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  1. Fachbereich Chemie der Universität Kaiserlautern, Erwin-Schrödinger Strasse, D-67663, Kaiserslautern, Germany

    Pia D. Vogel

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Vogel, P.D. Insights into ATP Synthase Structure and Function Using Affinity and Site-Specific Spin Labeling . J Bioenerg Biomembr 32, 413–421 (2000). https://doi.org/10.1023/A:1005536305526

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