1H NMR study on the interaction of cupric ion with ribonuclease A.
The reassignment of the 1H NMR C-2 histidine signals of the bovine pancreatic ribonuclease A has required a revision of the 1H NMR data on the role of the different histidines in their interaction with the Cu2+. The results of our measurements carried out at p2H 5.5 and 7.0 reduce the importance of His-12 as main site of interaction. At p2H 5.5 a very strong binding site involves His-119, while a weaker one contains certainly His-105. On the contrary, at p2H 7.0 the histidines 105 and 119 seem to possess binding constants of the same order of magnitude and in addition they provide stronger ligands for the Cu2+ than His-12. The comparison with X-ray data in the crystal shows numerous analogies. Finally, preliminary results on the competitive inhibition effect between the Cu2+ and 2',3'-cytidine monophosphoric acid are discussed.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003300:Copper / Q000378:metabolism*; D003563:Cyclic CMP / Q000378:metabolism; D006639:Histidine / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D010179:Pancreas / Q000201:enzymology; D011485:Protein Binding; D012260:Ribonucleases / Q000378:metabolism*
D003563:Cyclic CMP; D006639:Histidine; D003300:Copper; D012260:Ribonucleases