Siderophilin metal coordination. Difference ultraviolet spectroscopy of di-, tri-, and tetravalent metal ions with ethylenebis[(o-hydroxyphenyl)glycine].
Siderophilin metal coordination. Difference ultraviolet spectroscopy of di-, tri-, and tetravalent metal ions with ethylenebis[(o-hydroxyphenyl)glycine].
复制标题
亲铁素金属配位。
DOI:
10.1021/bi00527a040
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Raymond,KN
中科院分区:
文献类型:
--
作者:
Pecoraro,VL;Harris,WR;Carrano,CJ;Raymond,KN
Vincent L. Pecoraro, Wesley R. Harris, 1 Carl J. Carrano, 8 and Kenneth N. Raymond* abstract: So that the metal ion coordination site in the human iron transport protein, transferrin, could be probed, the complexation of a series of metal ions by the chelate analogue ethylenebis [(o-hydroxyphenyl) glycine](EHPG) has been studiedby difference UV spectroscopy, in which Ac values per coordinated phenol have been determined for the metal complex vs. the protonated form of the ligand. With the exception of the Cu2+ complex, maxima are observed at 242 and 290 nm with a minimum at 269 nm. The Ac values at 242 nm fall intotwo groups. Complexes of divalent metal ions (Zn2+, Cu2+, and Cd2+) have Ac values ranging from 5000 to 6600 M" 1 cm" 1 whereas larger Ac values are observed for complexes of tri-and tetravalent metal ions (Th4+, Ga3+, Fe3+, Ho3+, Eu3+, Er3+, Tb3+, and V02+), 7400-8700 M" 1 cm" 1. It is known that the transferrin binding sites contain tyrosyl residues, but there has been considerable debate concerning the precise number of tyrosine groups which bind to specific metal ions. Since it has been the common practice to assume that the Ac values for coordinationby all metal ions are identical, the larger range of Ac values actually observed here shows that such an assumption can actually lead to an erroneous tyrosine/metal site ratio. The difference spectra of