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- W2017166175 abstract "An ATPase complex sensitive to the energy transfer inhibitors oligomycin, dicyclohexylcarbodiimide and venturicidin has been solubilized from Rhodospirillum rubrum chromatophores with Triton X-100 and further purified by centrifugation on a glycerol gradient. The partially purified RrFo . F1 contains 13 distinct polypeptide subunits, as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, including the subunits of the oligomycin-sensitive, water-soluble RrF1 ATPase. The ATPase activity of RrF0 . F1 as that of the membrane-bound enzyme complex depends on Ca2+ or Mg2+ and from detailed kinetic studies it is concluded that the divalent cation-ATP complex is the substrate for both ATPase complexes. Free ATP and free Mg2+ act as competitive inhibitors, with Ki values of 1 mM and 7 muM, respectively. The subunit composition of the purified RrFo . F1 and its similarity to the membrane-bound ATPase with respect to cation dependence and sensitivity to energy transfer inhibitors suggests that it contains all the subunits of the R. rubrum coupling factor-ATPase complex." @default.
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- W2017166175 date "1979-10-01" @default.
- W2017166175 modified "2023-09-30" @default.
- W2017166175 title "Coupling factor ATPase complex of Rhodospirillum rubrum Purification and characterization of an oligomycin and N,N′-dicyclohexylcarbodiimide-sensitive (Ca2+ + Mg2+)-ATPase" @default.
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- W2017166175 doi "https://doi.org/10.1016/0005-2728(79)90191-9" @default.
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