The structure of bovine mitochondrial F1-ATPase: an example of rotary catalysis

A. G. Leslie, J. P. Abrahams, K. Braig, R. Lutter, R. I. Menz, G. L. Orriss, M. J. van Raaij, J. E. Walker

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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 languageEnglish
Pages (from-to)37-42
JournalBiochemical Society Transactions
Volume27
Issue number2
DOIs
Publication statusPublished - 1999

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