Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-O-(4-benzoyl)benzoyl adenosine 5'-diphosphate

Dudy Bar-Zvi, Marjorie A. Tiefert, Noun Shavit

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

The photoreactive nucleotide 3'-O-(4-benzoyl)benzoyl ADP (BzADP) is not a substrate for photophosphorylation but is a strong competitive inhibitor (Ki 2-25μM) with respect to ADP and ATP in photophosphorylation or ATP hydrolysis and Pi-ATP exchange reactions, respectively. The analog binds tightly to the membrane-bound CF1, 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.

Original languageEnglish
Pages (from-to)233-238
JournalFEBS Letters
Volume160
Issue number1-2
DOIs
StatePublished - 22 Aug 1983

Keywords

  • ATPase
  • Analog
  • Chloroplast
  • Photoaffinity labeling
  • Tightly-bound nucleotide

Fingerprint

Dive into the research topics of 'Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-O-(4-benzoyl)benzoyl adenosine 5'-diphosphate'. Together they form a unique fingerprint.

Cite this