| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1942635 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2011 | 8 Pages |
Abstract
âºKinetic approach reveals the different steps of inhibitory peptide IF1 binding to F0F1-ATPase. âºYeast IF1 fused in Nter with a 8 kDa globular polypeptide readily inhibits F1-ATPase. âºIF1 mid-part binds to αβ interface before its Nter part wraps around γ subunit. âºResidues 14-15-16 of yeast IF1 help to stabilize the ATPase-IF1 inhibited complex. âºPhenylalanine marking the beginning of IF1 mid-part is not mandatory for inhibition.
Keywords
yIF1PVDFF0F1-ATPaseF1-ATPaseTCAPMFTRISFCCPIF1SDSNi-NTA2-(N-morpholino)ethanesulfonic acidATP synthasetrichloracetic acidTris(hydroxymethyl)aminomethaneSMPSubmitochondrial particlessodium dodecyl sulfateBinding kineticsYeastMeSMitochondriaProtonmotive forcenickel-nitrilotriacetic acidPolyvinylidene fluorideInhibitory peptidecarbonyl cyanide-p-trifluoromethoxyphenylhydrazone
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Authors
Tiona Andrianaivomananjaona, Martin Moune-Dimala, Sameh Herga, Violaine David, Francis Haraux,