Proton translocation driven by ATP hydrolysis in V‐ATPases

FEBS Letters

Forgac, Michael¹  Nishi, Tsuyoshi¹  Kawasaki-Nishi, Shoko¹ 

[1] Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, USA

关键词: V-ATPase;    Vacuolar acidification;    Proton transport;    ATP hydrolysis;    Mechanism;    V-ATPases;    vacuolar proton-translocating adenosine triphosphatases;    F-ATPases;    F1F0 ATP synthases;   

DOI  :  10.1016/S0014-5793(03)00396-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (V₁) responsible for ATP hydrolysis and an integral domain (V₀) responsible for proton translocation. Based upon their structural similarity to the F₁F₀ ATP synthases, the V-ATPases are thought to operate by a rotary mechanism in which ATP hydrolysis in V₁ drives rotation of a ring of proteolipid subunits in V₀. This review is focused on the current structural knowledge of the V-ATPases as it relates to the mechanism of ATP-driven proton translocation.

【 授权许可】

Unknown