Characterization of Nucleotide Binding Sites on Isolated Chloroplast ATPase by Modification with 7-Chloro-4-Nitro-Benzofurazan

  • S. Bickel-Sandkötter
  • P. Strümper

Abstract

The nucleotide binding sites on CF1 have been widely studied. Catalytic sites as well as “tight” binding sites are found to be located on the β-subunits of CF1 or between α- and β-subunits (1). Binding of ADP (ATP) involves two recognition areas: One on the phosphate chain (2) and the other one on the base moiety, which includes the C2, N1, C6-region of the base (3). Essential residues like the aminogroup of lysine (4) or arginine take part in recognition of the negatively charged Pα of the phosphate chain. The hydroxyl residue of tyrosine most probably forms an H-bridge to the base N1.

Keywords

Slow Phase Nucleotide Binding Site Base Moiety Phosphate Chain Essential Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Xue, Z., Zhou, J.M., Melese, T., Cross, R.L. and Boyer, P.D. (1987) Biochemistry 26, 3749–3753PubMedCrossRefGoogle Scholar
  2. 2.
    Bickel-Sandkötter, S. (1985) Biochim. Biophys. Acta 809, 117–124CrossRefGoogle Scholar
  3. 3.
    Schlimme, E., de Groot, E.J., Schott, E., Strotmann, H. and Edelmann, K. (1979) FEBS Lett. 106, 251–256PubMedCrossRefGoogle Scholar
  4. 4.
    Bickel-Sandkötter, S. and Gokus, M. (1989) Biochim. Biophys. Acta 974, 30–35CrossRefGoogle Scholar
  5. 5.
    Sutton, R. and Ferguson, S.J. (1984) Eur. J. Biochem. 142, 387–392PubMedCrossRefGoogle Scholar
  6. 6.
    Andrews, W.W., Hill, F.C. and Allison, W.S. (1984) J. Biol. Chem. 259, 8219–8225PubMedGoogle Scholar
  7. 7.
    Ferguson, S.J., Lloyd, W.J. and Radda, G.K. (1975) Eur. J. Biochem. 54, 127–133PubMedCrossRefGoogle Scholar
  8. 8.
    Leckband, D. and Hammes, G.G. (1987) Biochemistry 26, 2306–2312PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • S. Bickel-Sandkötter
    • 1
  • P. Strümper
    • 1
  1. 1.Institut für Biochemie der PflanzenHeinrich-Heine-Universität DüsseldorfDüsseldorfGermany

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