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The Unfolding of a Catalytic Mechanism for the Remarkable ATP Synthase

  • Teri Mélèse
Part of the NATO ASI Series book series (NSSA, volume 91)

Abstract

In the past two decades, investigators in the field of bioenergetics have shown that a particular multisubunit protein complex (the ATP synthase) on the inner membrane of mitochondria, and on plant and bacterial membranes uses the energy supplied by an electrochemical or pH gradient to drive the net synthesis of ATP (see Figure 1). This energy could exert its effect either indirectly through a physical change in the structure of the protein itself (i.e. a conformational change) which would facilitate changes at the catalytic site, or directly, by the active donation of protons into the catalytic site which would be used in the covalent bond step when ATP is formed from ADP and Pi. Mitchell (1974, 1978) has suggested that effective removal of an oxygen group from Pi could be accomplished by such protonations at the catalytic site. However, over the past 10 years, increasing evidence has accrued showing that the energy provided by electron transport down the respiratory chain is used indirectly for the phosphorylation of ADP by Pi.

Keywords

Oxidative Phosphorylation Catalytic Subunit Catalytic Site Succinic Anhydride Submitochondrial Particle 
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

© Plenum Press, New York 1985

Authors and Affiliations

  • Teri Mélèse
    • 1
  1. 1.Department of Chemistry and BiochemistryUniversity of CaliforniaLos AngelesUSA

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