Woodworth R C
J Inorg Biochem. 1986 Oct-Nov;28(2-3):245-51. doi: 10.1016/0162-0134(86)80088-5.
High-resolution proton magnetic resonance spectra of the C-terminal half-molecule of ovotransferrin (OTf/2C) clearly resolve the C(2)H resonances of the five histidinyl residues in the protein. Formation of the Ga(III)OTf/2C(anion) ternary complexes results in different chemical shift and titration behaviors for certain C(2)H resonances in the carbonato, oxalato, and malonato complexes. The pKa' of the imidazole group involved in a proton relay with the synergistic anion and a water of hydration appears to be anion independent. Thus the initial attack of a proton on the ternary complex appears to be at a ligand other than the anion or anion-binding imidazole group.
卵转铁蛋白（OTf/2C）C端半分子的高分辨率质子磁共振谱清晰地分辨出该蛋白质中五个组氨酸残基的C(2)H共振。Ga(III)OTf/2C（阴离子）三元配合物的形成导致碳酸根、草酸根和丙二酸根配合物中某些C(2)H共振出现不同的化学位移和滴定行为。与协同阴离子和一个水化水分子进行质子传递的咪唑基团的pKa'似乎与阴离子无关。因此，质子对三元配合物的初始攻击似乎发生在阴离子或阴离子结合咪唑基团以外的配体上。
