10.1146/annurev.biochem.66.1.717
Crossref journal-article
Annual Reviews
Annual Review of Biochemistry (22)
Abstract

An X-ray structure of the F1 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 F1 and F0 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.

Bibliography

Boyer, P. D. (1997). THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE. Annual Review of Biochemistry, 66(1), 717–749.

Authors 1
  1. Paul D. Boyer (first)
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Dates
Type When
Created 23 years ago (July 27, 2002, 7:42 a.m.)
Deposited 3 years, 10 months ago (Oct. 5, 2021, 7:59 a.m.)
Indexed 1 day, 16 hours ago (Aug. 20, 2025, 9:14 a.m.)
Issued 28 years, 2 months ago (June 1, 1997)
Published 28 years, 2 months ago (June 1, 1997)
Published Print 28 years, 2 months ago (June 1, 1997)
Funders 0

None

@article{Boyer_1997, title={THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE}, volume={66}, ISSN={1545-4509}, url={http://dx.doi.org/10.1146/annurev.biochem.66.1.717}, DOI={10.1146/annurev.biochem.66.1.717}, number={1}, journal={Annual Review of Biochemistry}, publisher={Annual Reviews}, author={Boyer, Paul D.}, year={1997}, month=jun, pages={717–749} }