Characterization of the copper(II) binding site in the pink copper binding protein CusF by electron paramagnetic resonance spectroscopy

被引:12
作者
Astashkin, AV
Raitsimring, AM
Walker, FA
Rensing, C
McEvoy, MM [1 ]
机构
[1] Univ Arizona, Dept Biochem & Mol Biophys, Tucson, AZ 85721 USA
[2] Univ Arizona, Dept Chem, Tucson, AZ 85721 USA
[3] Univ Arizona, Dept Soil Water & Environm Sci, Tucson, AZ 85721 USA
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2005年 / 10卷 / 03期
基金
美国国家科学基金会;
关键词
copper homeostasis; electron paramagnetic resonance spectroscopy;
D O I
10.1007/s00775-005-0631-y
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Electron paramagnetic resonance (EPR) spectroscopy has been used to structurally characterize the copper-binding site in CusF protein from Escherichia coli. The EPR spectra indicate a single type II copper center with parameters typical for nitrogen and oxygen ligands (A(parallel to)similar to 200 G, g(parallel to)similar to 2.186, g(perpendicular to)similar to 2.051). The pulsed EPR data show that one of the ligands to Cu2+ is an imidazole ring of a histidine residue. The remote amino nitrogen of this imidazole ring is readily observed by electron spin-echo envelope modulation spectroscopy, while the imino nitrogen that is directly coordinated to the Cu2+ ion is observed by pulsed electron-nuclear double resonance (ENDOR). In addition, the ENDOR spectra reveal the presence of one more nitrogen ligand that was assigned to be a deprotonated peptide nitrogen. Apart from the two nitrogen ligands, it has been established that there are two nearby hydroxyl protons, although whether these belong to a single equatorial water ligand or two equatorial hydroxide ligands is not known.
引用
收藏
页码:221 / 230
页数:10
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