Abstract
Catalytic and noncatalytic sites of the chloroplast coupling factor (CF1) were selectively modified by incubation with the dialdehyde derivative of fluorescent adenosine diphosphate analog 1,N6-ethenoadenosine diphosphate. The modified CF1 was reconstituted with EDTA-treated thylakoid membranes of chloroplasts. The effects of light-induced transmembrane proton gradient and phosphate ions on the fluorescence of 1,N6-ethenoadenosine diphosphate, covalently bound to the catalytic sites of ATP synthase, were studied. Quenching of fluorescence of covalently bound 1,N6-ethenoadenosine diphosphate was observed under illumination of thylakoid membranes with saturating white light. Addition of inorganic phosphate to the reaction mixture in the dark increased the fluorescence of the label. Quenching reappeared under repeated illumination; however, addition of phosphate ions had no effect on the fluorescence yield in this case. When 1,N6-ethenoadenosine diphosphate was covalently bound to noncatalytic sites of ATP synthase, no similar fluorescence changes were observed. The relation between the observed changes of 1,N6-ethenoadenosine diphosphate fluorescence and the mechanism of energy-dependent structural changes in the catalytic site of ATP synthase is discussed.
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Abbreviations
- ɛADP:
-
1,N 6-ethenoadenosine diphosphate
- Pi :
-
inorganic phosphate
References
A. E. Senior, S. Nadanaciva, and J. Weber, Biochim. Biophys. Acta 1553, 188–211 (2002).
J. P. Abrahams, A. G. M. Leslie, R. Lutter, and J. E. Walker, Nature 370, 621–628 (1994).
S. Engelbrecht, Program RasMol V2 (http://131.173.28.71/se/sel.html).
A. N. Malyan and H. Strotmann, Photosynth. Res. 61, 1–9 (1999).
A. N. Tikhonov, A. F. Pogrebnaya, and Yu. M. Romanovskii, Biofizika 48(6), 1052–1070 (2003).
U. Pick and E. Racker, J. Biol. Chem. 254, 2793 (1979).
I. B. Minkov and H. Strotmann, Z. Naturforsch., A: Phys. Sci. 46, 621 (1991).
R. I. Feldman and D. S. Sigman, J. Biol. Chem. 257, 1676–1683 (1982).
G. Kothen, O. Schwarz, and H. Strotmann, Photosynth. Res. 2, 661 (1992).
S. K. Sytnik and A. N. Mal’yan, Biokhimiya (Moscow) 48(6), 890 (1983).
A. N. Mal’yan and S. K. Sytnik, Biokhimiya (Moscow) 49(6), 933–937 (1984).
Y. Shahak, D. V. Chipman, and N. Shavit, FEBS Lett. 33, 293–296 (1973).
N. P. Tatarintsev and A. D. Makarov, Biokhimiya (Moscow) 45(11), 1194–1197 (1980).
L. C. Cantley and G. G. Hammes, Biochemistry 14, 2976–2981 (1975).
L. C. Cantley and G. G. Hammes, Biochemistry 15, 1–8 (1976).
H. Strotman and S. Bickell-Sandkotter, Biochim. Biophys. Acta 460, 126–135 (1977).
D. I. Arnon, Plant Physiol. 24, 1–5 (1949).
A. Binder, A. T. Jagendorf, and E. Ngo, J. Biol. Chem. 253, 3094–3100 (1978).
A. N. Malyan and W. S. Allison, Biochim. Biophys. Acta 1554, 153–158 (2002).
M. M. Bradford, Anal. Biochem. 72, 248–254 (1976).
S. B. Easterbrock-Smith, J. S. Wallace, and D. B. Keech, Eur. J. Biochem. 62, 125–130 (1976).
Z. Xue and P. D. Boyer, Eur. J. Biochem. 179, 677–681 (1989).
V. Shoshan and N. Shavit, Eur. J. Biochem. 37, 355–360 (1973).
G. Schmidt and P. Gruber, Biochim. Biophys. Acta 808, 45 (1985).
H.-J. Schafer, H. W. Muller, and K. Dose, Biochem. Biophys. Res. Commun. 95, 1113–1118 (1980).
T. Melese, Z. Xue, K. E. Stempel, and P. D. Boyer, J. Biol. Chem. 263, 5833 (1988).
F. E. Possmayer, A. F. Hartog, J. A. Berden, and P. Graber, Biochim. Biophys. Acta 1510, 378–400 (2001).
C. M. Edel, A. F. Hartog, and J. A. Berden, Biochim. Biophys. Acta 1142, 327 (1993).
J. Weber and A. E. Senior, Biochim. Biophys. Acta 1319, 19–58 (1997).
D. Lohse, R. Thelen, and H. Strotmann, Biochim. Biophys. Acta 976, 85 (1989).
R. I. Mena, J. E. Walker, and A. G. Leslie, Cell 106, 331 (2001).
J. A. Secrist III, J. R. Barrio, N. J. Leonard, and G. Weber, Biochemistry 11, 3499–3506 (1972).
L. A. Blumenfeld, Problems of Biological Physics (Nauka, Moscow, 1977) [in Russian].
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Original Russian Text © N.P. Tatarintsev, A.N. Malyan, 2006, published in Biofizika, 2006, Vol. 51, No. 2, pp. 282–287.
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Tatarintsev, N.P., Malyan, A.N. Covalent Binding of 1,N 6-ethenoadenosine diphosphate to catalytic and noncatalytic sites of chloroplast ATP synthase. BIOPHYSICS 51, 241–246 (2006). https://doi.org/10.1134/S0006350906020138
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DOI: https://doi.org/10.1134/S0006350906020138