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- W2050825293 abstract "Two ADP binding sites have been demonstrated on the reconstitutively active β‐subunit, that was removed from the Rhodospirillum rubrum membrane‐bound ATP synthase. One is a high affinity site ( K d = 0.7 μM) that does not require MgCl 2 and is unaffected by it. The second is a low affinity binding site ( K d = 80 μM) that is absolutely dependent on MgCl 2 . For stable binding of ADP to this site, MgCl 2 must be present not only during the binding step but also during the elution‐centrifugation step used to separate the β‐subunit bound [ 3 H]ADP from the free ligand. When MgCl 2 is removed together with the free ligand [ 3 H]ADP dissociates very rapidly from this second binding site." @default.
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- W2050825293 date "1984-12-03" @default.
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- W2050825293 title "Demonstration of two binding sites for ADP on the isolated β-subunit of the <i>Rhodospirillum rubrum</i> R<sub>1</sub> F<sub>0</sub> F<sub>1</sub> -ATP synthase" @default.
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- W2050825293 doi "https://doi.org/10.1016/0014-5793(84)81229-6" @default.
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