6533b7d0fe1ef96bd125af65

RESEARCH PRODUCT

Photoaffinity cross-linking of F1ATPase from spinach chloroplasts by 3'-arylazido-beta-alanyl-8-azido ATP.

Gabriele RathgeberRichard J. BerzbornAchim SchuhenHans-jochen Schäfer

subject

Nucleotide binding siteAzidesChloroplastsStereochemistryPhotochemistryAffinity labelATPaseBiophysicsBiochemistryChloroplastF1ATPasechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyVegetablesGeneticsBinding siteChenopodiaceaeInterfacial localizationMolecular BiologyPhotoaffinity cross-linkingchemistry.chemical_classificationbiologyfood and beveragesAffinity LabelsCell Biologybiology.organism_classificationChloroplastProton-Translocating ATPasesEnzymeCross-Linking Reagentschemistrybiology.proteinSpinach chloroplastAdenosine triphosphate

description

UV irradiation of the ATPase (CF1) from spinach chloroplasts in the presence of 3'-arylazido-beta-alanyl-8-azido ATP (8,3'-DiN3ATP) results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of alpha-beta cross-links. The results demonstrate an interfacial localization of the nucleotide binding sites on CF1.

yearjournalcountryeditionlanguage
1994-03-07FEBS letters
10.1016/0014-5793(94)80151-7https://pubmed.ncbi.nlm.nih.gov/8131856