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Interaction of adenine nucleotides with the coupling factor of spinach chloroplasts A hydrogen—deuterium exchange study
Author(s) -
Nabedryk-Viala E.,
Calvet P.,
Thiéry J.M.,
Galmiche J.M.,
Girault G.
Publication year - 1977
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(77)80369-4
Subject(s) - deuterium , hydrogen–deuterium exchange , coupling (piping) , chloroplast , adenine nucleotide , chemistry , nucleotide , hydrogen , spinach , biochemistry , biophysics , biology , physics , materials science , nuclear physics , organic chemistry , metallurgy , gene
Hydrogen exchange is a sensitive method for detecting subtle structural changes that may occur when a ligand binds to a protein [l-5] . In the present paper we compare the interaction of coupling factor 1 with different adenine nucleotides (AMP, ADP, EATP, ATP) by means of hydrogendeuterium exchange measurements to get information about the compactness of the liganded and unliganded forms. Coupling factor 1 is a five-subunit enzymatic protein [6] which catalyses the formation of ATP from ADP and inorganic phosphate during photosynthesis. Circular dichroism or fluorescence measurements [7,8] indicate that the interaction of CF1 is equally strong with ATP, eATP, or ADP but absent with AMP and that it corresponds to a nucleotide binding on three sites of CFI . The present results also show that all of the nucleotides studied, except AMP, increase the conformational stability of the enzyme.