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The rotor in the membrane of the ATP synthase and relatives
Author(s) -
Arechaga Ignacio,
Jones Phil C
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02300-6
Subject(s) - atp synthase , atp synthase gamma subunit , chemiosmosis , atpase , v atpase , rotor (electric) , domain (mathematical analysis) , f atpase , chemistry , molecular machine , biochemistry , molecular motor , biophysics , biology , microbiology and biotechnology , enzyme , atp hydrolysis , physics , genetics , gene , chloroplast , quantum mechanics , mathematical analysis , mathematics , thylakoid
In recent years, structural information on the F 1 sector of the ATP synthase has provided an insight into the molecular mechanism of ATP catalysis. The structure strongly supports the proposal that the ATP synthase works as a rotary molecular motor. Insights into the membrane domain have just started to emerge but more detailed structural information is needed if the molecular mechanism of proton translocation coupled to ATP synthesis is to be understood. This review will focus mainly on the ion translocating rotor in the membrane domain of the F‐type ATPase, and the related vacuolar and archaeal relatives.