2,8-Diazido-ATP--a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1 in ATP synthase (from thermophilic bacteria PS3)
FEBS letters. Bd. 377. H. 3. Amsterdam u.a.: Elsevier 1995 S. 408 - 412
Erscheinungsjahr: 1995
ISBN/ISSN: 0014-5793
Publikationstyp: Zeitschriftenaufsatz
Sprache: Englisch
Doi/URN: 10.1016/0014-5793(95)01383-0
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Inhaltszusammenfassung
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-DiN3ATP). UV irradiation of the F1-ATPase (TF1) from the thermophilic bacterium PS3 in the presence of 2,8-DiN3ATP results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of alpha-beta crosslinks. The results confirm an interfacial localization of a...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-DiN3ATP). UV irradiation of the F1-ATPase (TF1) from the thermophilic bacterium PS3 in the presence of 2,8-DiN3ATP results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of alpha-beta crosslinks. The results confirm an interfacial localization of all the nucleotide binding sites on TF1.» weiterlesen» einklappen
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Klassifikation
DDC Sachgruppe:
Biowissenschaften, Biologie
