Abstract
ATP synthase is conceived as a rotatory engine with two reversible drives, the proton‐transporting membrane portion, F0, and the catalytic peripheral portion, F1. They are mounted on a central shaft (subunit γ) and held together by an eccentric bearing. It is established that the hydrolysis of three molecules of ATP in F1 drives the shaft over a full circle in three steps of 120° each. Proton flow through F0 probably generates a 12‐stepped rotation of the shaft so that four proton‐translocating steps of 30° each drive the synthesis of one molecule of ATP. We addressed the elasticity of the transmission between F0 and F1 in a model where the four smaller steps in F0 load a torsional spring which is only released under liberation of ATP from F1. The kinetic model of an elastic ATP synthase described a wealth of published data on the synthesis/hydrolysis of ATP by F0F1 and on proton conduction by F0 as function of the pH and the protonmotive force. The pK values of the proton‐carrying group interacting with the acidic and basic sides of the membrane were estimated as 5.3–6.4 and 8.0–8.3, respectively.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 25, 2002, 1:52 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 9:50 p.m.) |
Indexed | 2 weeks, 1 day ago (Aug. 6, 2025, 9:02 a.m.) |
Issued | 26 years, 4 months ago (April 16, 1999) |
Published | 26 years, 4 months ago (April 16, 1999) |
Published Online | 26 years, 4 months ago (April 16, 1999) |
Published Print | 26 years, 4 months ago (April 16, 1999) |
@article{Cherepanov_1999, title={Transient accumulation of elastic energy in proton translocating ATP synthase}, volume={449}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(99)00386-5}, DOI={10.1016/s0014-5793(99)00386-5}, number={1}, journal={FEBS Letters}, publisher={Wiley}, author={Cherepanov, Dmitry A. and Mulkidjanian, Armen Y. and Junge, Wolfgang}, year={1999}, month=apr, pages={1–6} }