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The Relationship Between the Structure and Catalytic Mechanism of the Chloroplast ATP Synthase

  • Mark L. Richter
  • Denise A. Mills
Part of the Advances in Photosynthesis and Respiration book series (AIPH, volume 4)

Summary

An overview of the nucleotide binding properties and current models of the catalytic mechanism of the chloroplast ATP synthase is presented. The discussion includes consideration of the role of the small subunits of the catalytic chloroplast coupling factor 1 (CF1) in gating the flow of protons across the membrane. Some emphasis is placed on the potential role of the ε subunit in a proton-driven activation process and an apparent role of this subunit in influencing cooperativity among the different nucleotide binding sites on both membrane-bound and isolated CF1 Controversy over the type of nucleotide binding sites on CF1 is discussed, together with the potential involvement of the different nucleotide binding sites in the catalytic process.

Keywords

Nucleotide Binding Coupling Factor Nucleotide Binding Site Spinach Chloroplast Rhodospirillum Rubrum 
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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Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • Mark L. Richter
    • 1
  • Denise A. Mills
    • 1
  1. 1.Department of BiochemistryThe University of KansasLawrenceUSA

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