scholarly journals Dimerization of Bovine F1-ATPase by Binding the Inhibitor Protein, IF1

2000 ◽  
Vol 275 (37) ◽  
pp. 28353-28355 ◽  
Author(s):  
Elena Cabezón ◽  
Ignacio Arechaga ◽  
P. Jonathan ◽  
G. Butler ◽  
John E. Walker
Keyword(s):  
Inhibitor Protein ◽  
F1 Atpase

scholarly journals Inhibition sites in F1-ATPase from bovine heart mitochondria

2005 ◽  
Vol 386 (3) ◽  
pp. 591-598 ◽  
Author(s):  
Jonathan R. GLEDHILL ◽  
John E. WALKER
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Inhibitor Protein ◽  
Ischaemia Reperfusion Injury ◽  
F1 Atpase ◽  
Amphiphilic Peptides ◽  
Rational Development ◽  
Bacterial Enzyme ◽  
Inhibitory Site ◽  
Natural Inhibitor

High-resolution crystallographic studies of a number of inhibited forms of bovine F1-ATPase have identified four independent types of inhibitory site: the catalytic site, the aurovertin B-binding site, the efrapeptin-binding site and the site to which the natural inhibitor protein IF1 binds. Hitherto, the binding sites for other inhibitors, such as polyphenolic phytochemicals, non-peptidyl lipophilic cations and amphiphilic peptides, have remained undefined. By employing multiple inhibition analysis, we have identified the binding sites for these compounds. Several of them bind to the known inhibitory sites. The amphiphilic peptides melittin and synthetic analogues of the mitochondrial import pre-sequence of yeast cytochrome oxidase subunit IV appear to mimic the natural inhibitor protein, and the polyphenolic phytochemical inhibitors resveratrol and piceatannol compete for the aurovertin B-binding site (or sites). The non-peptidyl lipophilic cation rhodamine 6G acts at a separate unidentified site, indicating that there are at least five inhibitory sites in the F1-ATPase. Each of the above inhibitors has significantly different activity against the bacterial Bacillus PS3 α3β3γ subcomplex compared with that observed with bovine F1-ATPase. IF1 does not inhibit the bacterial enzyme, even in the absence of the ε-subunit. An understanding of these inhibitors may enable rational development of therapeutic agents to act as novel antibiotics against bacterial ATP synthases or for the treatment of several disorders linked to the regulation of the ATP synthase, including ischaemia–reperfusion injury and some cancers.

Pressure Effects on the Interaction between Natural Inhibitor Protein and Mitochondrial F1–ATPase

1998 ◽  
Vol 349 (2) ◽  
pp. 304-312 ◽  
Author(s):  
Luz A.M.G. Fornells ◽  
Horacio Guimarães-Motta ◽  
Jorge Saad Nehme ◽  
Orlando B. Martins ◽  
Jerson L. Silva
Keyword(s):  
Pressure Effects ◽  
Inhibitor Protein ◽  
F1 Atpase ◽  
Natural Inhibitor

scholarly journals S1.15 The mechanism of inhibition of bovine F1-ATPase by the inhibitor protein IF1

2008 ◽  
Vol 1777 ◽  
pp. S12
Author(s):  
John V. Bason ◽  
Grace Li ◽  
Michael J. Runswick ◽  
Martin G. Montgomery ◽  
John E. Walker
Keyword(s):  
Inhibitor Protein ◽  
F1 Atpase ◽  
Mechanism Of Inhibition

scholarly journals Modulation of the Oligomerization State of the Bovine F1-ATPase Inhibitor Protein, IF1, by pH

2000 ◽  
Vol 275 (33) ◽  
pp. 25460-25464 ◽  
Author(s):  
Elena Cabezon ◽  
P. Jonathan G. Butler ◽  
Michael J. Runswick ◽  
John E. Walker
Keyword(s):  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase

Inhibitors of the catalytic domain of mitochondrial ATP synthase

2006 ◽  
Vol 34 (5) ◽  
pp. 989-992 ◽  
Author(s):  
J.R. Gledhill ◽  
J.E. Walker
Keyword(s):  
Atp Synthase ◽  
Binding Sites ◽  
Catalytic Domain ◽  
Structural Studies ◽  
Inhibitor Protein ◽  
X Ray ◽  
F1 Atpase ◽  
X Ray Crystallography ◽  
Mitochondrial Atp Synthase ◽  
Natural Inhibitor

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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