2003/04/18 by Shoko Kawasaki-Nishi, Tsuyoshi Nishi, Michael Forgac · 88 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #ATP Synthase and ATPases Research #Mitochondrial Function and Pathology #Photosynthetic Processes and Mechanisms #ATP hydrolysis #ATPase #Chemiosmosis #ATP synthase #Biophysics #Proton #Proton transport #Chemistry #Intracellular #Hydrolysis #Electrochemical gradient #Proton pump #Intracellular pH #Biochemistry #Stereochemistry #Enzyme #Biology #Membrane #Physics
paper · doi:10.1016/s0014-5793(03)00396-x
published in FEBS Letters 545(1), 76-85 (Wiley)
openalex publication_date 2003/04/18 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
The vacuolar H(+)-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are multisubunit complexes composed of a peripheral domain (V(1)) responsible for ATP hydrolysis and an integral domain (V(0)) responsible for proton translocation. Based upon their structural similarity to the F(1)F(0) ATP synthases, the V-ATPases are thought to operate by a rotary mechanism in which ATP hydrolysis in V(1) drives rotation of a ring of proteolipid subunits in V(0). This review is focused on the current structural knowledge of the V-ATPases as it relates to the mechanism of ATP-driven proton translocation.