Abstract
There is now compelling evidence in support of a rotary catalytic mechanism in F1-ATPase, and, by extension, in the intact ATP synthase. Although models have been proposed to explain how protein translocation in F0 results in rotation of the gamma-subunit relative to the alpha 3/beta 3 assembly in F1 [22], these are still speculative. It seems likely that a satisfactory explanation of this mechanism will ultimately depend on structural information on the intact ATP synthase
Original language | English |
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Pages (from-to) | 37-42 |
Journal | Biochemical Society Transactions |
Volume | 27 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1999 |