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Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′‐ O ‐(4‐benzoyl)benzoyl adenosine 5'‐diphosphate
Author(s) -
Bar-Zvi Dudy,
Tiefert Marjorie A.,
Shavit Noun
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80973-9
Subject(s) - photophosphorylation , chemistry , nucleotide , atp hydrolysis , adenosine diphosphate , enzyme , adenosine triphosphate , covalent bond , substrate (aquarium) , biochemistry , adenine nucleotide , nucleoside diphosphate kinase , stereochemistry , chloroplast , atpase , biology , organic chemistry , platelet aggregation , platelet , ecology , immunology , gene
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 CF 1 , 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.