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Photoaffinity cross‐linking of F 1 ATPase from the thermophilic bacterium PS3 by 3′‐arylazido‐β‐alanyl‐2‐azido ATP
Author(s) -
Schäfer Hans-Jochen,
Rathgeber Gabriele,
Dose Klaus,
Kagawa Yasuo
Publication year - 1989
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(89)80972-x
Subject(s) - photoaffinity labeling , nucleotide , bifunctional , atpase , thermophile , chemistry , stereochemistry , biochemistry , binding site , enzyme , gene , catalysis
The photoactivatable bifunctional 3′‐arylazido‐β‐alanyl‐2‐azido ATP (2,3′‐DiN 3 ATP) has been applied to study the localization of the nucleotide‐binding sites of coupling factor 1 (F 1 ATPase, TF 1 ) from the thermophilic bacterium PS3 by photoaffinity cross‐linking. UV irradiation of TF 1 in the presence of 2,3′‐DiN 3 ATP results in the nucleotide‐dependent formation of various higher molecular mass cross‐links formed by two, three or even four α‐ and/or β‐subunits. The differences observed upon photoaffinity cross‐linking by the bifunctional 2‐azido ATP or 8‐azido ATP analog are discussed. They are probably due to the varied maximal distance between both azido groups, or to the different conformations ( anti/syn ) of these analogs. The results confirm our suggestion that several (possibly all) nucleotide‐binding sites of F 1 ATPases are located at the interfaces between α‐ and β‐subunits.