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. 1971 Sep;68(9):2181–2184. doi: 10.1073/pnas.68.9.2181

A Soluble Mitochondrial ATP Synthetase Complex Catalyzing ATP-Phosphate and ATP-ADP Exchange

Robert J Fisher †, Jenn C Chen †, B P Sani †, Suresh S Kaplay †, D Rao Sanadi *,*
PMCID: PMC389380  PMID: 5289378

Abstract

The highly purified soluble ATP synthetase complex from mitochondria, containing energy-transfer Factor A (the terminal ADP phosphorylation enzyme of oxidative phosphorylation) and Factor D, catalyzes ATP-Pi and ATP-ADP exchange reactions. The ATP-Pi exchange activity is inhibited by low concentrations of the uncouplers of oxidative phosphorylation, oligomycin and p-chloromercnriphenylsulfonate. It is stimulated threefold by dithiothreitol and is Mg++ dependent. Antiserum to coupling factor 1 (F1) also inhibits the ATP-Pi exchange. The ATP-ADP exchange activity appears to be greater than the ATP-Pi exchange activity. The results suggest that the nonphosphorylated high-energy intermediate (X∼C), and possibly the phosphorylated intermediate (X∼P), are formed on the synthetase. Sites of uncoupler and oligomycin action reside in the terminal ATP synthetase.

Keywords: oligomycin, p-chloromercuriphenylsulfonate, high-energy intermediate, uncoupling

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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