Specificity of nucleotide binding sites in isolated chloroplast coupling factor (CF1)

Menahem Banai; Noun Shavit; David M. Chipman

doi:10.1016/0005-2728(78)90009-9

Specificity of nucleotide binding sites in isolated chloroplast coupling factor (CF₁)

Menahem Banai
, Noun Shavit
, David M. Chipman

Department of Life Sciences

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

12 Scopus citations

Abstract

The binding of various nucleotides to chloroplast coupling factor CF₁ was studied by two dialysis techniques. It was found that the number of nucleoside diphosphate sites and their specificities for the base moiety is dependent on the magnesium concentration. In the presence of 50 μM added MgCl₂, the protein has a single strong site/mol protein with K_d = 0.5 μM for ADP and high specificity (K_d > 20 μM for ε{lunate}ADP, GDP, CDP). In the presence of 5 mM MgCl₂, the protein has two independent tight ADP sites (K_d = 0.4 μM) of low specificity (K_d ≈ 0.8, 2, and 2 μrmM, respectively for ε{lunate}ADP, GDP, and CDP). These results are compared with the specificity of the partial reactions for photophosphorylation.

Original language	English
Pages (from-to)	100-107
Number of pages	8
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	504
Issue number	1
DOIs	https://doi.org/10.1016/0005-2728(78)90009-9
State	Published - 11 Oct 1978

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

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title = "Specificity of nucleotide binding sites in isolated chloroplast coupling factor (CF1)",

abstract = "The binding of various nucleotides to chloroplast coupling factor CF1 was studied by two dialysis techniques. It was found that the number of nucleoside diphosphate sites and their specificities for the base moiety is dependent on the magnesium concentration. In the presence of 50 μM added MgCl2, the protein has a single strong site/mol protein with Kd = 0.5 μM for ADP and high specificity (Kd > 20 μM for ε\{lunate\}ADP, GDP, CDP). In the presence of 5 mM MgCl2, the protein has two independent tight ADP sites (Kd = 0.4 μM) of low specificity (Kd ≈ 0.8, 2, and 2 μrmM, respectively for ε\{lunate\}ADP, GDP, and CDP). These results are compared with the specificity of the partial reactions for photophosphorylation.",

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T1 - Specificity of nucleotide binding sites in isolated chloroplast coupling factor (CF1)

AU - Banai, Menahem

AU - Shavit, Noun

AU - Chipman, David M.

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Y1 - 1978/10/11

N2 - The binding of various nucleotides to chloroplast coupling factor CF1 was studied by two dialysis techniques. It was found that the number of nucleoside diphosphate sites and their specificities for the base moiety is dependent on the magnesium concentration. In the presence of 50 μM added MgCl2, the protein has a single strong site/mol protein with Kd = 0.5 μM for ADP and high specificity (Kd > 20 μM for ε{lunate}ADP, GDP, CDP). In the presence of 5 mM MgCl2, the protein has two independent tight ADP sites (Kd = 0.4 μM) of low specificity (Kd ≈ 0.8, 2, and 2 μrmM, respectively for ε{lunate}ADP, GDP, and CDP). These results are compared with the specificity of the partial reactions for photophosphorylation.

AB - The binding of various nucleotides to chloroplast coupling factor CF1 was studied by two dialysis techniques. It was found that the number of nucleoside diphosphate sites and their specificities for the base moiety is dependent on the magnesium concentration. In the presence of 50 μM added MgCl2, the protein has a single strong site/mol protein with Kd = 0.5 μM for ADP and high specificity (Kd > 20 μM for ε{lunate}ADP, GDP, CDP). In the presence of 5 mM MgCl2, the protein has two independent tight ADP sites (Kd = 0.4 μM) of low specificity (Kd ≈ 0.8, 2, and 2 μrmM, respectively for ε{lunate}ADP, GDP, and CDP). These results are compared with the specificity of the partial reactions for photophosphorylation.

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JF - Biochimica et Biophysica Acta - Bioenergetics

IS - 1

ER -

Specificity of nucleotide binding sites in isolated chloroplast coupling factor (CF₁)

Abstract

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