Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-O-(4-benzoyl)benzoyl adenosine 5'-diphosphate

Dudy Bar-Zvi; Marjorie A. Tiefert; Noun Shavit

doi:10.1016/0014-5793(83)80973-9

Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-O-(4-benzoyl)benzoyl adenosine 5'-diphosphate

Dudy Bar-Zvi, Marjorie A. Tiefert, Noun Shavit

Department of Life Sciences

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

24 Scopus citations

Abstract

The photoreactive nucleotide 3'-O-(4-benzoyl)benzoyl ADP (BzADP) is not a substrate for photophosphorylation but is a strong competitive inhibitor (K_i 2-25μM) with respect to ADP and ATP in photophosphorylation or ATP hydrolysis and P_i-ATP exchange reactions, respectively. The analog binds tightly to the membrane-bound CF₁, competes with the right binding of ADP, and prevents the inactivation of the enzyme by tight binding of ADP. Upon irradiation with long wavelength ultraviolet light, the tightly bound BzADP becomes covalently attached to both the α- and β-subunits of the enzyme.

Original language	English
Pages (from-to)	233-238
Journal	FEBS Letters
Volume	160
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(83)80973-9
State	Published - 22 Aug 1983

Keywords

ATPase
Analog
Chloroplast
Photoaffinity labeling
Tightly-bound nucleotide

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-O-(4-benzoyl)benzoyl adenosine 5'-diphosphate",

abstract = "The photoreactive nucleotide 3'-O-(4-benzoyl)benzoyl ADP (BzADP) is not a substrate for photophosphorylation but is a strong competitive inhibitor (Ki 2-25μM) with respect to ADP and ATP in photophosphorylation or ATP hydrolysis and Pi-ATP exchange reactions, respectively. The analog binds tightly to the membrane-bound CF1, competes with the right binding of ADP, and prevents the inactivation of the enzyme by tight binding of ADP. Upon irradiation with long wavelength ultraviolet light, the tightly bound BzADP becomes covalently attached to both the α- and β-subunits of the enzyme.",

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AU - Tiefert, Marjorie A.

AU - Shavit, Noun

PY - 1983/8/22

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N2 - The photoreactive nucleotide 3'-O-(4-benzoyl)benzoyl ADP (BzADP) is not a substrate for photophosphorylation but is a strong competitive inhibitor (Ki 2-25μM) with respect to ADP and ATP in photophosphorylation or ATP hydrolysis and Pi-ATP exchange reactions, respectively. The analog binds tightly to the membrane-bound CF1, competes with the right binding of ADP, and prevents the inactivation of the enzyme by tight binding of ADP. Upon irradiation with long wavelength ultraviolet light, the tightly bound BzADP becomes covalently attached to both the α- and β-subunits of the enzyme.

AB - The photoreactive nucleotide 3'-O-(4-benzoyl)benzoyl ADP (BzADP) is not a substrate for photophosphorylation but is a strong competitive inhibitor (Ki 2-25μM) with respect to ADP and ATP in photophosphorylation or ATP hydrolysis and Pi-ATP exchange reactions, respectively. The analog binds tightly to the membrane-bound CF1, competes with the right binding of ADP, and prevents the inactivation of the enzyme by tight binding of ADP. Upon irradiation with long wavelength ultraviolet light, the tightly bound BzADP becomes covalently attached to both the α- and β-subunits of the enzyme.

KW - ATPase

KW - Analog

KW - Chloroplast

KW - Photoaffinity labeling

KW - Tightly-bound nucleotide

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Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-O-(4-benzoyl)benzoyl adenosine 5'-diphosphate

Abstract

Keywords

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