Analysis of the Nucleotide Binding Sites of ATP Synthase and Consequences for the Catalytic Mechanism

  • J. A. Berden
  • A. F. Hartog
Chapter

Abstract

The complexity of the mechanism of ATP hydrolysis and ATP synthesis by the ATP synthase is illustrated by the large number of nucleotide binding sites. Many efforts have been made to characterize all six binding sites and to analyze the role of the nucleotides at each site. In the present chapter we will describe, starting from some well-established facts concerning the properties of F1 (the hydrophilic part of the enzyme, containing all nucleotide binding sites), the results of studies on the nucleotide binding sites of the enzyme and draw some conclusions on the catalytic mechanism of ATP hydrolysis and synthesis. We will mainly describe studies with the mitochondrial system from bovine heart; however, where relevant, studies on the enzyme from other sources will be mentioned. At present, the subunit interactions and the conformational changes within the ATP synthase are studied in much detail in order to obtain a better insight into what really happens during catalysis. But conclusions on the precise mechanism of catalysis have to be in agreement with the properties of the nucleotide binding sites. Some features of the ATP synthase, considered to be well established, may serve as starting point for our analysis. We name the following:

Keywords

Catalytic Site Adenine Nucleotide Nucleotide Binding Site Bovine Heart Beef Heart 
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Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • J. A. Berden
    • 1
  • A. F. Hartog
    • 1
  1. 1.E. C. Slater Institute, BioCentrumUniversity of AmsterdamAmsterdamThe Netherlands

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