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EnglishThe properties of the mitochondrial F1FO-ATPase catalytic site, which can bind Mg2+, Mn2+, or Ca2+ and hydrolyze ATP, were explored by inhibition kinetic analyses to cast light on the Ca2+-activated F1FO-ATPase connection with the permeability transition pore (PTP) that initiates cascade events leading to cell death. While the natural cofactor Mg2+ activates the F1FO-ATPase in competition with Mn2+, Ca2+ is a noncompetitive inhibitor in the presence of Mg2+. Selective F-1 inhibitors (Is-F-1), namely NBD-Cl, piceatannol, resveratrol, and quercetin, exerted different mechanisms (mixed and uncompetitive inhibition) on either Ca2+- or Mg2+-activated F1FO-ATPase, consistent with the conclusion that the catalytic mechanism changes when Mg2+ is replaced by Ca2+. In a partially purified F-1 domain preparation, Ca2+-activated F-1-ATPase maintained Is-F-1 sensitivity, and enzyme inhibition was accompanied by the maintenance of the mitochondrial calcium retention capacity and membrane potential. The data strengthen the structural relationship between Ca2+-activated F1FO-ATPase and the PTP, and, in turn, on consequences, such as physiopathological cellular changes.
| Titolo: | Mitochondrial Ca2+ -activated F1 FO -ATPase hydrolyzes ATP and promotes the permeability transition pore |
| Autore/i: | Algieri, Cristina; Trombetti, Fabiana; Pagliarani, Alessandra; Ventrella, Vittoria; Bernardini, Chiara; Fabbri, Micaela; Forni, Monica; Nesci, Salvatore |
| Autore/i Unibo: | |
| Anno: | 2019 |
| Rivista: | |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1111/nyas.14218 |
| Abstract: | The properties of the mitochondrial F1FO-ATPase catalytic site, which can bind Mg2+, Mn2+, or Ca2+ and hydrolyze ATP, were explored by inhibition kinetic analyses to cast light on the Ca2+-activated F1FO-ATPase connection with the permeability transition pore (PTP) that initiates cascade events leading to cell death. While the natural cofactor Mg2+ activates the F1FO-ATPase in competition with Mn2+, Ca2+ is a noncompetitive inhibitor in the presence of Mg2+. Selective F-1 inhibitors (Is-F-1), namely NBD-Cl, piceatannol, resveratrol, and quercetin, exerted different mechanisms (mixed and uncompetitive inhibition) on either Ca2+- or Mg2+-activated F1FO-ATPase, consistent with the conclusion that the catalytic mechanism changes when Mg2+ is replaced by Ca2+. In a partially purified F-1 domain preparation, Ca2+-activated F-1-ATPase maintained Is-F-1 sensitivity, and enzyme inhibition was accompanied by the maintenance of the mitochondrial calcium retention capacity and membrane potential. The data strengthen the structural relationship between Ca2+-activated F1FO-ATPase and the PTP, and, in turn, on consequences, such as physiopathological cellular changes. |
| Data stato definitivo: | 2019-12-22T23:36:40Z |
| Appare nelle tipologie: | 1.01 Articolo in rivista |
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|---|---|---|---|---|
| Algieri_et_al-2019-postprint.pdf | Postprint | Licenza per accesso libero gratuito | Embargo: 24/08/2020 Contatta l'autore |
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