Abstract
The bovine heart mitochondrial F1-ATPase (MF1), which is composed of five different polypeptide chains in a subunit stoichiometry of α 3 β 3 γδε, has a total of six adenine nucleotide binding sites (Esch and Allison, 1979; Cross and Nalin, 1982). Kinetic evidence presented by Lardy’s laboratory (Lardy et al, 1975; Schuster et al., 1975) suggested the presence of regulatory sites that specifically bind adenine nucleotides and catalytic sites which are less specific and hydrolyze ATP, ITP, GTP and other nucleoside triphosphates. Gautheron and her colleagues (DiPietro et al, 1980; Baubichon et al., 1981; Fellous et al., 1984) have provided evidence for a regulatory site on the β subunit of MF1 which responds to ADP but not to GDP and GDP analogues.
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© 1989 Plenum Press, New York
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Allison, W.S., Verburg, J.G., Bullough, D.A. (1989). On the Number of Catalytic Sites in the F1-ATPase that Catalyze Steady State ATP Hydrolysis. In: Marzuki, S. (eds) Molecular Structure, Function, and Assembly of the ATP Synthases. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0593-4_25
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DOI: https://doi.org/10.1007/978-1-4613-0593-4_25
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