Search results for "Nucleotide binding site"

showing 3 items of 3 documents

2,8-Diazido-ATP — a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1 in ATP synthase (from thermophilic b…

1995

Abstract 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 α-β crosslinks. The results confirm an interfacial localization of all the nucleotide binding sites on TF1.

Models MolecularAzidesNucleotide binding siteLightStereochemistryImmunoblottingBiophysicsDirect interfacial localizationShort lengthBiochemistry8-azidoadenosine 5'-triphosphatechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyGeneticsNucleotide binding sitesBifunctionalMolecular BiologyThermophilic bacterium PS3Photoaffinity cross-linkingchemistry.chemical_classificationATP synthasebiologyBacteriaThermophileAffinity LabelsCell BiologyProton-Translocating ATPasesEnzymeCross-Linking ReagentsBiochemistrychemistrybiology.proteinF1-ATPase: Short-length bifunctional photoaffinity labelFEBS Letters
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Photoaffinity cross-linking of F1ATPase from spinach chloroplasts by 3'-arylazido-beta-alanyl-8-azido ATP.

1994

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.

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 triphosphateFEBS letters
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Photoaffinity labeling of the coupling factor 1 from the thermophilic bacterum PS3 by 8-azido ATP

1984

AbstractTo localize the nucleotide binding sites of the F1ATPase (TF1) from the thermophilic bacterium PS3 we have used 14C-labeled 8-azido ATP (8-N3ATP) as photoaffmity label. 8-N3ATP is hydrolyzed by the F,ATPase in the absence of ultraviolet light. Irradiation by ultraviolet light of the enzyme in the presence of 8-N3ATP results in reduction of ATPase activity and in preferential nucleotide specific labeling of the α subunits (0.8–0.9 mol 8-N3ATP/TF1,α:β = 4:1). Inactivation and labeling do not depend on the presence of Mg2+. Both effects decrease upon addition of various nucleotide di- or triphosphates.

chemistry.chemical_classificationPhotoaffinity labelingStereochemistryNoncatalytic nucleotide binding siteThermophileBiophysicsCell BiologyBiochemistryCoupling (electronics)HydrolysisEnzymechemistryStructural BiologyPhotoaffinity labelingMoleBacterial F1ATPaseGeneticsUltraviolet lightCatalytic nucleotide binding siteNucleotideThermophilic bacterium PS3Molecular BiologyFEBS Letters
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