Photoinactivation of the F1-ATPase from Spinach Chloroplasts by Dequalinium Is Accompanied by Derivatization of Methionine β183

Ren, Huimiao; Allison, William S.

doi:10.1074/jbc.272.51.32294

Cited by 9 publications

(3 citation statements)

References 46 publications

(69 reference statements)

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“…Dequalinium inhibits chloroplast Ca 2ϩ -ATPase, whereas it stimulates chloroplast Mg 2ϩ -ATPase (329). The inhibition of ATPase activity by dequalinium is reversible, hyperbolic, and noncompetitive for MF 1 and TF 1 in the dark (52,268,296,329,452).…”

Section: Amphiphilic Cationic Dyesmentioning

confidence: 98%

“…A long lag is observed in the inhibition of TF 1 by dequalinium that is not observed for the inhibition of MF 1 (296). Dequalinium, upon illumination at 350 nm, inactivates F 1 -ATPase with pseudo-first-order kinetics (296,329,452,454). This is accompanied by derivatization of ␤Phe420 in TF 1 (296), ␤Met183 in CF 1 (329), and ␣Phe403, ␣Phe406, and a side chain within residues 440 to 459 of the ␤ subunit in bovine heart MF 1 (454).…”

Section: Amphiphilic Cationic Dyesmentioning

confidence: 99%

“…Dequalinium is a quinoline derivative that inhibits the ATPase activities of F 1 from both mitochondria and bacteria (52,268,296,329,452). Dequalinium inhibits chloroplast Ca 2ϩ -ATPase, whereas it stimulates chloroplast Mg 2ϩ -ATPase (329).…”

Section: Amphiphilic Cationic Dyesmentioning

confidence: 99%

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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

275

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: Amphiphilic Cationic Dyesmentioning

confidence: 98%

Section: Amphiphilic Cationic Dyesmentioning

confidence: 99%

See 1 more Smart Citation

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

275

302

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The adenine pocket of a single catalytic site is derivatized when the bovine heart mitochondrial F1-ATPase is photoinactivated with 4-amino-1-octylquinaldinium

Grodsky

Allison

1999

Cell Biochem Biophys

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The bovine heart mitochondrial F1-ATPase (MF1) is reversibly inhibited in the dark by 4-amino-1-octylquinaldinium (AOQ) with an I0.5 value of 48 microM. When irradiated in the presence of AOQ, MF1 is photoinactivated with an apparent Kd of 12 microM. About 1.1 mol of [3H]AOQ were incorporated per mol of MF1 on complete photoinactivation. Fractionation of a cyanogen bromide digest of MF1 photolabeled with [3H]AOQ followed by fractionation of peptic digests of partially purified cyanogen bromide fragments led to isolation of two CNBr/peptic fragments labeled with 3H. Sequence analysis of the labeled peptides revealed that one contained residues 423-441 of the beta subunit. A gap in position 2 of the sequence indicates that beta Phe424 is derivatized. The phenyl side-chain of this residue is part of a pocket that binds the adenine moiety of ATP or ADP at catalytic sites. The other peptide, which was labeled to a greater extent, contained residues 342-358 of the beta subunit, but in this case, no gap was found in the sequence indicating that the derivatized amino-acid side-chain might not have survived the conditions of automatic Edman degradation. This peptide contains beta Tyr345, the side-chain of which is also a component of the pocket that binds the adenine moiety of ATP or ADP to catalytic sites. However, for the reason stated, there is no direct evidence that beta Tyr345 is labeled in this peptide.

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The effect of medium viscosity on kinetics of ATP hydrolysis by the chloroplast coupling factor CF1

Malyan

2016

Photosynth Res

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The coupling factor CF1 is a catalytic part of chloroplast ATP synthase which is exposed to stroma whose viscosity is many-fold higher than that of reaction mixtures commonly used to measure kinetics of CF1-catalyzed ATP hydrolysis. This study is focused on the effect of medium viscosity modulated by sucrose or bovine serum albumin (BSA) on kinetics of Ca(2+)- and Mg(2+)-dependent ATP hydrolysis by CF1. These agents were shown to reduce the maximal rate of Ca(2+)-dependent ATPase without changing the apparent Michaelis constant (К m), thus supporting the hypothesis on viscosity dependence of CF1 activity. For the sulfite- and ethanol-stimulated Mg(2+)-dependent reaction, the presence of sucrose increased К m without changing the maximal rate that is many-fold as high as that of Ca(2+)-dependent hydrolysis. The hydrolysis reaction was shown to be stimulated by low concentrations of BSA and inhibited by its higher concentrations, with the increasing maximal reaction rate estimated by extrapolation. Sucrose- or BSA-induced inhibition of the Mg(2+)-dependent ATPase reaction is believed to result from diffusion-caused deceleration, while its BSA-induced stimulation is probably caused by optimization of the enzyme structure. Molecular mechanisms of the inhibitory effect of viscosity are discussed. Taking into account high protein concentrations in the chloroplast stroma, it was suggested that kinetic parameters of ATP hydrolysis, and probably those of ATP synthesis in vivo as well, must be quite different from measurements taken at a viscosity level close to that of water.

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Photoinactivation of the F1-ATPase from Spinach Chloroplasts by Dequalinium Is Accompanied by Derivatization of Methionine β183

Cited by 9 publications

References 46 publications

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

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

The adenine pocket of a single catalytic site is derivatized when the bovine heart mitochondrial F1-ATPase is photoinactivated with 4-amino-1-octylquinaldinium

The effect of medium viscosity on kinetics of ATP hydrolysis by the chloroplast coupling factor CF1

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