The interaction of nucleotides with F1-ATPase inactivated with 4-chloro-7-nitrobenzofurazan

Gregory, R.E.; Recktenwald, Diether; Hess, Benno

doi:10.1016/0005-2728(81)90027-x

Cited by 11 publications

(2 citation statements)

References 23 publications

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“…It inhibits both the synthetic and hydrolytic activities of ATP synthases from bacteria, chloroplasts, and mitochondria by modifying an essential residue (␤Tyr311, bovine sequence) at the catalytic site(s) of F 1 (12,70,119,120,245,388,415). Depending on the experimental conditions, other subunits, particularly the ␣ subunit, are also modified by NBD-Cl (96,121,146,283). In F 1 modified by NBD-Cl, the Tyr-O-NBD linkage is unstable at alkaline pH.…”

Section: Cys and Tyr Residue Modifiersmentioning

confidence: 99%

ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas

Hong

Pedersen

2008

Microbiol Mol Biol Rev

276

302

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SUMMARY ATP synthase, a double-motor enzyme, plays various roles in the cell, participating not only in ATP synthesis but in ATP hydrolysis-dependent processes and in the regulation of a proton gradient across some membrane-dependent systems. Recent studies of ATP synthase as a potential molecular target for the treatment of some human diseases have displayed promising results, and this enzyme is now emerging as an attractive molecular target for the development of new therapies for a variety of diseases. Significantly, ATP synthase, because of its complex structure, is inhibited by a number of different inhibitors and provides diverse possibilities in the development of new ATP synthase-directed agents. In this review, we classify over 250 natural and synthetic inhibitors of ATP synthase reported to date and present their inhibitory sites and their known or proposed modes of action. The rich source of ATP synthase inhibitors and their known or purported sites of action presented in this review should provide valuable insights into their applications as potential scaffolds for new therapeutics for human and animal diseases as well as for the discovery of new pesticides and herbicides to help protect the world's food supply. Finally, as ATP synthase is now known to consist of two unique nanomotors involved in making ATP from ADP and Pi, the information provided in this review may greatly assist those investigators entering the emerging field of nanotechnology.

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Section: Cys and Tyr Residue Modifiersmentioning

confidence: 99%

ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas

Hong

Pedersen

2008

Microbiol Mol Biol Rev

276

302

View full text Add to dashboard Cite

show abstract

“…At pH 9, the tyrosine-bound Nbf was transferred intramolecularly to a nitrogen group in the 13 subunit to form a stable derivative, N-Nbf-FI (173). Nbf also reacted with a 13 subunit in yeast mitochondrial F \ (174), and in F \ from E. coli (175) , R. rub rum (176), and chloroplasts (177). ATPase activity was restored by the addition of sulfhydryl compounds, such as N-acetylcysteine, glutathione, and di thiothreitol to O-Nbf-F\; the absorption at 385 nm decreased concomitantly and that at 425 nm increased, owing to the displacement of the Nbf residue from the phenolic group of tyrosine and the formation of a Nbf-thiol derivative with the added thiols .…”

Section: Chemical Modifiers Of a Tp Synthasementioning

confidence: 99%