THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE

1997/06/01 by Paul D. Boyer · 5 citations
Biochemistry, Genetics and Molecular Biology · #ATP Synthase and ATPases Research #Mitochondrial Function and Pathology #Photosynthetic Processes and Mechanisms

paper · doi:10.1146/annurev.biochem.66.1.717

openalex publication_date 1997/06/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

Abstract

An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanism with an internal rotation of the gamma 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 gamma subunit rotation have been achieved. The findings have implications for other enzymatic catalyses.

Citations

• The H+/ATP coupling ratio of the ATP synthase from thiol‐modulated chloroplasts and two cyanobacterial strains is four
• Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

Cited by

• Bacterial Chemotaxis: The Early Years of Molecular Studies
• Function and Structure of Complex II of the Respiratory Chain
• Structure of the mitochondrial ATP synthase by electron cryomicroscopy
• ATP synthase — a marvellous rotary engine of the cell
• Oxidative phosphorylation [wikipedia]