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2,8‐Diazido‐ATP — a short‐length bifunctional photoaffinity label for photoaffinity cross‐linking of a stable F 1 in ATP synthase (from thermophilic bacteria PS3)
Author(s) -
HansJochen Schäfer,
Gabriele Rathgeber,
Yasuo Kagawa
Publication year - 1995
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(95)01383-0
Subject(s) - nucleotide , photoaffinity labeling , thermophile , bifunctional , atp synthase , atpase , enzyme , chemistry , biochemistry , affinity label , stereochemistry , binding site , gene , catalysis
To demonstrate the direct interfacial position of nucleotide binding sites between subunits of proteins we have synthesized the bifunctional photoaffinity label 2,8‐diazidoadenosine 5′‐triphosphate (2,8‐DiN 3 ATP). UV irradiation of the F 1 ‐ATPase (TF 1 ) from the thermophilic bacterium PS3 in the presence of 2,8‐DiN 3 ATP results in a nucleotide‐dependent inactivation of the enzyme and in a nucleotide‐dependent formation of α‐β crosslinks. The results confirm an interfacial localization of all the nucleotide binding sites on TF 1 .