Abstract
An understanding of the mechanism of ATP synthase requires an explanation of how inhibitors act. The catalytic F1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states. Four independent inhibitory sites have been identified by high-resolution structural studies. They are the catalytic site, and the binding sites for the antibiotics aurovertin and efrapeptin and for the natural inhibitor protein, IF1.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 25, 2006, 9:28 a.m.) |
Deposited | 3 years, 9 months ago (Nov. 17, 2021, 5:04 p.m.) |
Indexed | 1 month, 1 week ago (July 24, 2025, 7:55 a.m.) |
Issued | 18 years, 11 months ago (Oct. 1, 2006) |
Published | 18 years, 11 months ago (Oct. 1, 2006) |
Published Online | 18 years, 10 months ago (Oct. 25, 2006) |
Published Print | 18 years, 11 months ago (Oct. 1, 2006) |
@article{Gledhill_2006, title={Inhibitors of the catalytic domain of mitochondrial ATP synthase}, volume={34}, ISSN={1470-8752}, url={http://dx.doi.org/10.1042/bst0340989}, DOI={10.1042/bst0340989}, number={5}, journal={Biochemical Society Transactions}, publisher={Portland Press Ltd.}, author={Gledhill, J.R. and Walker, J.E.}, year={2006}, month=oct, pages={989–992} }