Demonstration of two binding sites for ADP on the isolated β-subunit of the Rhodospirillum rubrum R1F0F1-ATP synthase

Daniel Khananshvili, Zippora Gromet-Elhanan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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 (Kd = 0.7 μM) that does not require MgCl2 and is unaffected by it. The second is a low affinity binding site (Kd = 80 μM) that is absolutely dependent on MgCl2. For stable binding of ADP to this site, MgCl2 must be present not only during the binding step but also during the elution-centrifugation step used to separate the β-subunit bound [3H]ADP from the free ligand. When MgCl2 is removed together with the free ligand [3H]ADP dissociates very rapidly from this second binding site.

Original languageEnglish
Pages (from-to)10-14
Number of pages5
JournalFEBS Letters
Volume178
Issue number1
DOIs
StatePublished - 3 Dec 1984
Externally publishedYes

Keywords

  • Rhodospirillum rubrum FF-ATPsynthase β-Subunit ADP-binding site MgCl dependence Binding affinity

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