Selenite ameliorates the ATP hydrolysis of mitochondrial F 1 F O -ATPase by changing the redox state of thiol groups and impairs the ADP phosphorylation.

Autor: Algieri C; Department of Veterinary Medical Sciences, Alma Mater Studiorum-University of Bologna, 40064, Ozzano Emilia, Italy., Oppedisano F; Department of Health Sciences, Institute of Research for Food Safety and Health (IRC-FSH), University 'Magna Græcia' of Catanzaro, 88100, Catanzaro, Italy., Trombetti F; Department of Veterinary Medical Sciences, Alma Mater Studiorum-University of Bologna, 40064, Ozzano Emilia, Italy., Fabbri M; Department of Veterinary Medical Sciences, Alma Mater Studiorum-University of Bologna, 40064, Ozzano Emilia, Italy., Palma E; Department of Health Sciences, Institute of Research for Food Safety and Health (IRC-FSH), University 'Magna Græcia' of Catanzaro, 88100, Catanzaro, Italy., Nesci S; Department of Veterinary Medical Sciences, Alma Mater Studiorum-University of Bologna, 40064, Ozzano Emilia, Italy. Electronic address: salvatore.nesci@unibo.it.
Jazyk: angličtina
Zdroj: Free radical biology & medicine [Free Radic Biol Med] 2024 Jan; Vol. 210, pp. 333-343. Date of Electronic Publication: 2023 Dec 04.
DOI: 10.1016/j.freeradbiomed.2023.11.041
Abstrakt: Selenite as an inorganic form of selenium can affect the redox state of mitochondria by modifying the thiol groups of cysteines. The F 1 F O -ATPase has been identified as a mitochondrial target of this compound. Indeed, the bifunctional mechanism of ATP turnover of F 1 F O -ATPase was differently modified by selenite. The activity of ATP hydrolysis was stimulated, whereas the ADP phosphorylation was inhibited. We ascertain that a possible new protein adduct identified as seleno-dithiol (-S-Se-S-) mercaptoethanol-sensitive caused the activation of F-ATPase activity and the oxidation of free -SH groups in mitochondria. Conversely, the inhibition of ATP synthesis by selenite might be irreversible. The kinetic analysis of the activation mechanism was an uncompetitive mixed type with respect to the ATP substrate. Selenite bound more selectively to the F 1 F O -ATPase loaded with the substrate by preferentially forming a tertiary (enzyme-ATP-selenite) complex. Otherwise, the selenite was a competitive mixed-type activator with respect to the Mg 2+ cofactor. Thus, selenite more specifically bound to the free enzyme forming the complex enzyme-selenite. However, even if the selenite impaired the catalysis of F 1 F O -ATPase, the mitochondrial permeability transition pore phenomenon was unaffected. Therefore, the reversible energy transduction mechanism of F 1 F O -ATPase can be oppositely regulated by selenite.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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