The mechanochemistry of V-ATPase proton pumps
The mechanochemistry of V-ATPase proton pumps
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DOI：
10.1016/s0006-3495(00)76823-8
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发表时间：
2000-06-01
影响因子：
3.4
通讯作者：
Oster, G
中科院分区：
文献类型：
--
作者：
Grabe, M;Wang, HY;Oster, G
液泡H+-ATP酶（V-ATP酶）是一类结构上与F-ATP酶相似的质子泵。这两个蛋白质家族的特征在于负责质子易位的膜结合片段（V-0，F-0）和通过水解ATP为易位提供能量的可溶性部分（V-1，F-1）。在这里，我们提出了一个机械化学模型的功能的V-0离子泵，是符合已知的结构特征和生物化学。该模型再现了各种性能的实验测量，并提供了一个统一的观点，细胞内pH调节的许多机制。
The vacuolar H+-ATPases (V-ATPases) are a universal class of proton pumps that are structurally similar to the F-ATPases. Both protein families are characterized by a membrane-bound segment (V-0, F-0) responsible for the translocation of protons, and a soluble portion, (V-1, F-1), which supplies the energy for translocation by hydrolyzing ATP. Here we present a mechanochemical model for the functioning of the V-0 ion pump that is consistent with the known structural features and biochemistry. The model reproduces a variety of experimental measurements of performance and provides a unified view of the many mechanisms of intracellular pH regulation.