Abstract
ATP synthase mediates proton flow through its membrane portion, F 0 , which drives the synthesis of ATP in its headpiece, F 1 . The F 1 -portion contains a hexagonal array of three subunits α and three β encircling a central subunit γ, that in turn interacts with a smaller ɛ and with F 0 . Recently we reported that the application of polarized absorption recovery after photobleaching showed the ATP-driven rotation of γ over at least two, if not three, β. Here we extend probes of such rotation aided by a new theory for assessing continuous versus stepped, Brownian versus unidirectional molecular motion. The observed relaxation of the absorption anisotropy is fully compatible with a unidirectional and stepping rotation of γ over three equidistantly spaced angular positions in the hexagon formed by the alternating subunits α and β. The results strongly support a rotational catalysis with equal participation of all three catalytic sites. In addition we report a limited rotation of γ without added nucleotides, perhaps idling and of Brownian nature, that covers only a narrow angular domain.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 10:40 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 3:58 p.m.) |
Indexed | 2 weeks, 4 days ago (Aug. 6, 2025, 9:21 a.m.) |
Issued | 28 years, 3 months ago (April 29, 1997) |
Published | 28 years, 3 months ago (April 29, 1997) |
Published Online | 28 years, 3 months ago (April 29, 1997) |
Published Print | 28 years, 3 months ago (April 29, 1997) |
@article{Sabbert_1997, title={Functional and idling rotatory motion within F 1 -ATPase}, volume={94}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.94.9.4401}, DOI={10.1073/pnas.94.9.4401}, number={9}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Sabbert, D. and Engelbrecht, S. and Junge, W.}, year={1997}, month=apr, pages={4401–4405} }