Crossref journal-article
Portland Press Ltd.
Biochemical Society Transactions (288)
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.

Bibliography

Gledhill, J. R., & Walker, J. E. (2006). Inhibitors of the catalytic domain of mitochondrial ATP synthase. Biochemical Society Transactions, 34(5), 989–992.

Authors 2
  1. J.R. Gledhill (first)
  2. J.E. Walker (additional)
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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)
Funders 0

None

@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} }