Ligand-induced conformational changes of citrate synthase studied with the fluorescent probe 8-anilinonaphthalene 1-sulfonate.
Experiments are presented which show that oxaloacetate and analogs thereof with (R)-malate substructure, on interaction with citrate synthase linked to synthase 8-anilinonaphthalene 1-sulfonate (ANS), induce identical conformational changes of a characteristic magnitude. A conformational change of lower magnitude is also produced on binding of CoASH or ATP to citrate synthase.ANS and is completed on addition of oxaloacetate. The significance of these ligand-dependent conformational changes is discussed.
Kollmann-Koch
A
A
Institut für Physiologische Chemie der Technischen Universität München, Federal Republic of Germany.
Eggerer
H
H
D000817:Anilino Naphthalenesulfonates; D000818:Animals; D001665:Binding Sites; D002950:Citrate (si)-Synthase / Q000378:metabolism*; D005456:Fluorescent Dyes; D008024:Ligands; D010071:Oxaloacetates / Q000378:metabolism*; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013552:Swine; D013997:Time Factors
D000817:Anilino Naphthalenesulfonates; D005456:Fluorescent Dyes; D008024:Ligands; D010071:Oxaloacetates; C027132:1-anilino-8-naphthalenesulfonate; D002950:Citrate (si)-Synthase; D007652:Oxo-Acid-Lyases