6533b85afe1ef96bd12b8e24
RESEARCH PRODUCT
Energy-Linked Reactions Catalyzed by the Purified ATPase Complex (F0F1) from Rhodospirillum rubrum Chromatophores
Klaus DoseErwin SchneiderPeter FriedlUdo Schwulérasubject
OligomycinMacromolecular SubstancesBiologyRhodospirillum rubrumBiochemistryFluorescenceMembrane Lipidschemistry.chemical_compoundAdenosine TriphosphateMoietyAdenosine Triphosphataseschemistry.chemical_classificationLiposomeQuenching (fluorescence)Cell-Free SystemUncoupling AgentsATPase complexRhodospirillum rubrumMembrane ProteinsBacterial Chromatophoresbiology.organism_classificationFluorescenceMolecular WeightEnzymeSolubilitychemistryBiochemistryLiposomesdescription
1. The isolation of the F0F1-ATPase complex from Rhodospirillum rubrum chromatophores by the use of taurodeoxycholate is described. 2. The enzyme preparation contains about 12 polypeptides; five are subunits of the F1 moiety. 3. The ATPase activity of the purified enzyme is dependent on the addition of phospholipids. 4. Km-vales for Mg2+-ATP and Ca2+-ATP are similar to the values obtained for the membrane-bound enzyme. 5. The F0F1-ATPase complex is more than 70% inhibited by oligomycin and N,N′-dicyclohexyl-carbodiimide. 6. The F0F1-ATPase complex was integrated into liposomes. The reconstituted proteoliposomes catalyzed energy transduction as shown by ATP-dependent quenching of acridine dye fluorescence and ATP-32Pi exchange.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1980-07-01 | European Journal of Biochemistry |