F1-ATPase-catalyzed synthesis of ATP from oleoylphosphate and ADP.
AUTOR(ES)
Johnston, R
RESUMO
Purified preparations of F1-ATPase (ATP phosphohydrolase; EC 3.6.1.3) isolated from yeast mitochondria catalyze the reaction of oleoylphosphate with ADP to yield ATP and oleic acid. Formation of ATP is specifically inhibited by the F1-ATPase inhibitor 1799 and by dinitrophenol. In the presence of F1, dinitrophenol "uncouples" the synthase reaction by causing rapid hydrolysis of oleoylphosphate without ATP formation. It is proposed that this F1 catalyzed ATP synthesis reaction corresponds to the terminal chemical step in oxidative phosphorylation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=432068Documentos Relacionados
- Phosphoryl Group Exchange between ATP and ADP Catalyzed by H+-ATPase from Oat Roots.
- Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants.
- The structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride
- The 2.8-Å structure of rat liver F1-ATPase: Configuration of a critical intermediate in ATP synthesis/hydrolysis
- Sequence of the F0-atpase proteolipid (atp9) gene from rice mitochondria.