Forward operation of adenine nucleotide translocase during F0F1-ATPase reversal: critical role of matrix substrate-level phosphorylation.

@article{Chinopoulos2010ForwardOO,
  title={Forward operation of adenine nucleotide translocase during F0F1-ATPase reversal: critical role of matrix substrate-level phosphorylation.},
  author={Christos Chinopoulos and Akos A. Gerencser and Mikl{\'o}s M{\'a}ndi and Katalin M{\'a}th{\'e} and Be{\'a}ta T{\"o}r{\"o}csik and Judit D{\'o}czi and Lilla Turi{\'a}k and Gergely Kiss and Csaba Konr{\`a}d and Szilvia Vajda and Vikt{\'o}ria Vereczki and Richard J. Oh and Vera {\'A}d{\'a}m-Vizi},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2010},
  volume={24 7},
  pages={2405-16}
}
In pathological conditions, F(0)F(1)-ATPase hydrolyzes ATP in an attempt to maintain mitochondrial membrane potential. Using thermodynamic assumptions and computer modeling, we established that mitochondrial membrane potential can be more negative than the reversal potential of the adenine nucleotide translocase (ANT) but more positive than that of the F(0)F(1)-ATPase. Experiments on isolated mitochondria demonstrated that, when the electron transport chain is compromised, the F(0)F(1)-ATPase… CONTINUE READING

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