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pH-Dependent Changes in ATP and ADP Affinity for the Tight Nucleotide-Binding Site of the Chloroplast Coupling Factor CF1

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Current Research in Photosynthesis

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Abstract

The ATPase complex of chloroplasts (H+-ATPase, ATP-synthase) carries out synthesis (hydrolysis) of ATP coupled with transmembrane transport of hydrogen ions. This complex consists of a hydrophytic catalytic part called coupling factor CF1, and a hydrophobic part, CF0, the function of which is to translocate protons towards CF1. CF1 can bind as many as six nucleotide molecules /1/. After CF1 precipitation by ammonium sulfate with subsequent gel filtration, the enzyme retains about 1 mol of tightly bound nucleotides consisting mainly of ADP /2/.

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Author information

Authors and Affiliations

  1. Inst. of Soil Science and Photosynthesis, Acad. Sci. USSR, 142292, Pushchino, Moscow Region, USSR

    A. N. Malyan & O. I. Vitseva

Authors
  1. A. N. Malyan
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  2. O. I. Vitseva
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, University of Stockholm, Stockholm, Sweden

    M. Baltscheffsky

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Malyan, A.N., Vitseva, O.I. (1990). pH-Dependent Changes in ATP and ADP Affinity for the Tight Nucleotide-Binding Site of the Chloroplast Coupling Factor CF1 . In: Baltscheffsky, M. (eds) Current Research in Photosynthesis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0511-5_453

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  • DOI: https://doi.org/10.1007/978-94-009-0511-5_453

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6716-4

  • Online ISBN: 978-94-009-0511-5

  • eBook Packages: Springer Book Archive

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