Probing the metal site in Rhus vernicifera stellacyanin by Ni(II) substitution and paramagnetic NMR spectroscopy

被引：13

作者：

Fernandez, CO

Sannazzaro, AI

Diaz, LE

Vila, AJ ^{[1
]}

机构：

[1] Univ Nacl Rosario, Area Biofis, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario, Argentina

[2] Univ Buenos Aires, Fac Farm & Bioquim, LANAIS RMN 300, RA-1113 Buenos Aires, DF, Argentina

来源：

INORGANICA CHIMICA ACTA | 1998年 / 273卷 / 1-2期

关键词：

paramagnetic NMR; blue copper proteins; stellacyanin; nickel complexes; metalloprotein complexes;

D O I：

10.1016/S0020-1693(97)06073-8

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Stellacyanin from Rhus vernificera is a blue copper protein in which the metal is coordinated to a Cys, two His and a Gin residue. We have studied the Ni(II) derivative of stellacyanin by paramagnetic H-1 NMR spectroscopy. The NMR spectrum resembles that of Ni(II) Met121Gln azurin, indicating a similar coordination environment. The hyperfine signals were assigned by means of 1D and 2D NOE spectroscopy. Evidence is obtained which indicates that the Gln residue is bound to the metal through its oxygen atom. (C) 1998 Elsevier Science S.A. All rights reserved.

引用

页码：367 / 371

页数：5

共 32 条

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ADMAN ET, 1991, ADV PROTEIN CHEM, V42, P144

[2] H-1 NOE STUDIES ON DICOPPER(II) DICOBALT(II) SUPEROXIDE-DISMUTASE [J].