THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE

DOI Web Site 101 Citations
  • Paul D. Boyer
    Molecular Biology Institute, University of California, Los Angeles, California 90095-1570

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<jats:p> An X-ray structure of the F<jats:sub>1</jats:sub> portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic β subunits that support the binding change mechanism with an internal rotation of the γ subunit. Other structural and mutational probes of the F<jats:sub>1</jats:sub> and F<jats:sub>0</jats:sub> portions of the ATP synthase are reviewed, together with kinetic and other evaluations of catalytic site occupancy and behavior during hydrolysis or synthesis of ATP. Subunit function as related to proton translocation and rotational catalysis is considered. Physical demonstrations of the γ subunit rotation have been achieved. The findings have implications for other enzymatic catalyses. </jats:p>

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