Pause and rotation of F 1 -ATPase during catalysis
- 13 November 2001
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 98 (24) , 13649-13654
- https://doi.org/10.1073/pnas.241365698
Abstract
F 1 -ATPase is a rotary motor enzyme in which a single ATP molecule drives a 120° rotation of the central γ subunit relative to the surrounding α 3 β 3 ring. Here, we show that the rotation of F 1 -ATPase spontaneously lapses into long (≈30 s) pauses during steady-state catalysis. The effects of ADP-Mg and mutation on the pauses, as well as kinetic comparison with bulk-phase catalysis, strongly indicate that the paused enzyme corresponds to the inactive state of F 1 -ATPase previously known as the ADP-Mg inhibited form in which F 1 -ATPase fails to release ADP-Mg from catalytic sites. The pausing position of the γ subunit deviates from the ATP-waiting position and is most likely the recently found intermediate 90° position.Keywords
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