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

Daniel Khananshvili; Zippora Gromet-Elhanan

doi:10.1016/0014-5793(84)81229-6

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

Weizmann Institute of Science

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

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 MgCl₂ and is unaffected by it. The second is a low affinity binding site (K_d = 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 language	English
Pages (from-to)	10-14
Number of pages	5
Journal	FEBS Letters
Volume	178
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(84)81229-6
State	Published - 3 Dec 1984
Externally published	Yes

Funding

Funders	Funder number
Minerva Foundation Munich/FRG

Keywords

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

Access to Document

10.1016/0014-5793(84)81229-6

Cite this

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

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.",

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AB - 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.

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