@article{3dc280fa5788474ba126e72c2b9f3ef2,
title = "Features of V-ATPases that distinguish them from F-ATPases",
abstract = "The general structure of F- and V-ATPases is quite similar and they may share a common mechanism of action that involves mechanochemical energy transduction. Both holoenzymes are composed of catalytic sectors, F1 and V1 respectively, and membrane sectors, Fo and Vo respectively. Although we assume that a similar mechanism underlies ATP-dependent proton pumping by F- and V-ATPases in eukaryotic cells, the latter cannot catalyze pmf-driven ATP synthesis. The loss of this ability is probably due to a proton slip that is a consequence of alterations in its membrane sector. The major events include gene duplication of the proteolipids and the presence of three distinct proteolipids in each complex.",
keywords = "F-ATPase, Proteolipid, Slip mechanism, V-ATPase",
author = "Natalie Perzov and Vered Padler-Karavani and Hannah Nelson and Nathan Nelson",
note = "Funding Information: This project has been funded by the BMBF and supported by BMBF{\textquoteright}s International Bureau at the DLR.",
year = "2001",
month = aug,
day = "31",
doi = "10.1016/S0014-5793(01)02709-0",
language = "אנגלית",
volume = "504",
pages = "223--228",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "3",
}