Ultraviolet difference spectroscopy of myoglobin: assignment of pK values of tyrosyl phenolic groups and the stability of the ferryl derivatives.
Ultraviolet difference spectroscopy of myoglobin: assignment of pK values of tyrosyl phenolic groups and the stability of the ferryl derivatives.
复制标题
肌红蛋白的紫外差光谱:酪氨酰酚基的 pK 值分配和 Ferryl 衍生物的稳定性。
DOI:
10.1021/bi00510a045
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Peisach,J
中科院分区:
文献类型:
--
作者:
Uyeda,M;Peisach,J
M. Uyeda* and J. Peisach* abstract: The ionization of tyrosyl phenolic groups of ferric myoglobins from red kangaroo, horse, and sperm whale has been studied by pH difference spectroscopy at 245 nm. As the number of tyrosyl residues in these proteins varies mon-otonically from one to three, respectively, we are able to make pK assignments for all of them. The apparent pK for tyro-sine-146, an invariant residue in all myoglobins, is unusually high, 12.7-12.9, as this residue is in a hydrophobic region of the molecule and the tyrosyl phenolic group is hydrogen bonded to the peptide carbonyl of isoleucine-99. For the ferric cyanide and the oxy forms of the various myoglobins, this apparent pX is elevated by about 0.5 pH unit while in the deoxy proteins, it does not change significantly. A second tyrosine, at position 103, is found in the horse and sperm whale proteins, but not in the kangaroo protein. It has a significantly lower apparent pK than is observed for Tyr-146 in all the derivatives studied. A third tyrosyl residue, at position 151, is exclusive to the sperm whale protein and has an apparent pK of 10.3, almost equivalent to thatof tyrosine in aqueous solution. The apparent pATs for the ferryl forms of the three