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Structure of F0F1ATPases Determined by Direct and Indirect Methods

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Membrane Protein Structure

Part of the book series: Methods in Physiology Series ((METHPHYS))

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Abstract

ATP synthesis—the phosphorylation of ADP by inorganic phosphate (P;) in mitochondria, chloroplast, and bacteria—is a very important and complex biochemical pathway. The reaction involves the utilization of the proton electrochemical gradient, produced by either the oxidation of substrates or the utilization of light quanta, for the generation of ATP levels up to 108 times the concentration expected from the hydrolytic equilibrium (ATP + H2O = ADP + P i ). The reaction in which the dissipation of the H+ gradient is coupled to the phosphorylation of ADP is carried out by a large, complex enzyme system: the ATP synthase. The membranes of bacteria, chloroplasts, and mitochondria contain ATP synthases that utilize H+ gradients generated across their membranes for the formation of as much as 98% of the ATP required by living organisms. All the ATP synthases are composed of two main sectors: the integral membrane portion Fo and the membrane associated portion F1 (see reviews by Futai and Kanazawa, 1983; Futai et al., 1989; Senior, 1990; Kagawa, 1984). Both Fo and F1 are multisubunit proteins. (At least thirteen subunits have been identified in mammalian ATP synthases (Hatefi, 1985; Godinot & Di Pietro, 1986; Walker et al., 1987), while only eight subunits exist in bacteria (Filligame, 1981; Schneider and Altendorf, 1987). It has been demonstrated that Fo forms a transmembrane H+ channel that directs H+ ions to the F1 sector where their translocation is coupled to the synthesis of ATP. The F1 sector contains all the catalytic and noncatalytic nucleotide-binding sites. ATP synthases have been the subject of extensive structural studies that utilized direct and indirect methods aimed at providing three-dimensional structural information about the enzyme. The most relevant and recent studies will be discussed in this chapter; no attempt is made to make this a comprehensive review of all the ATP synthase literature.

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  1. L. Mario Amzel
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  2. Mario A. Blanchet
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  3. Peter L. Pedersen
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Editors and Affiliations

  1. College of Medicine, Department of Physiology and Biophysics, University of California, Irvine, Irvine, California, USA

    Stephen H. White Ph.D. (Professor of Physiology and Biophysics) (Professor of Physiology and Biophysics)

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© 1994 American Physiological Society

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Amzel, L.M., Blanchet, M.A., Pedersen, P.L. (1994). Structure of F0F1ATPases Determined by Direct and Indirect Methods. In: White, S.H. (eds) Membrane Protein Structure. Methods in Physiology Series. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-7515-6_7

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  • DOI: https://doi.org/10.1007/978-1-4614-7515-6_7

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