-
- Paul D. Boyer
- Molecular Biology Institute, University of California, Los Angeles, California 90095-1570
説明
<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>
収録刊行物
-
- Annual Review of Biochemistry
-
Annual Review of Biochemistry 66 (1), 717-749, 1997-06
Annual Reviews
