Cobalt(II) as an NMR probe for the investigation of the coordination sites of conalbumin.
The bis and mono cobalt(II) derivatives of conalbumin in the presence of bicarbonate have been prepared. The 1H NMR spectra have been recorded at 60 MHz. Well-shaped isotropically shifted signals in the range -100 to +100ppm have been observed for both the mono and bis cobalt(II) derivatives; besides the intensity, all the isotropically shifted signals for the two derivatives are superimposable, indicating that the two sites are so similar as to be indistinguishable within the resolution of the technique. With the aid of T1 measurements, the signals have been assigned to the protons of two histidine and two tyrosinate ligands. The spectra are consistent with six-coordinated, high-spin cobalt(II) chromophores with two trans tyrosinate moieties at each site.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D003035:Cobalt; D003207:Conalbumin; D004527:Egg Proteins; D009682:Magnetic Resonance Spectroscopy; D008670:Metals; D009354:Neodymium; D011485:Protein Binding
D004527:Egg Proteins; D008670:Metals; D003207:Conalbumin; D009354:Neodymium; D003035:Cobalt