Assignment and analysis of fluorine nuclear magnetic resonance spectra of 4-fluorotryptophan myoglobins and hemoglobins.
Assignment and analysis of fluorine nuclear magnetic resonance spectra of 4-fluorotryptophan myoglobins and hemoglobins.
复制标题
4-氟色氨酸肌红蛋白和血红蛋白的氟核磁共振谱的归属和分析。
DOI：
10.1021/bi961664h
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Sligar,SG
中科院分区：
文献类型：
--
作者：
Pearson,JG;Montez,B;Le,H;Oldfield,E;Chien,EY;Sligar,SG
我们获得了通过定点诱变制备的野生型[4-F] Trp标记的肌红蛋白（MbCO、MbO 2、deoxyMb、metMb和MbCN）和血红蛋白（HbCO、HbO 2和deoxyHb）以及几种突变体（W7 F Mb、β W15 F Hb、β W37 S Hb和β Y130 F Hb，均为碳一氧加合物）的470 MHz 19 F NMR谱。观察到的折叠诱导的最大化学位移范围为6.4 ppm。使用多极屏蔽极化率-局部反应场方法，我们计算了静电场对氟屏蔽的贡献。对于没有F原子与相邻基团接触的残基，我们发现其位移与实验值的均方偏差为0.1ppm，HbCOA的R2-类结构与实验值非常接近雅阁。
We have obtained the 470 MHz19F NMR spectra of wild type [4-F]Trp-labeled myoglobins (MbCO, MbO2, deoxyMb, metMb, and MbCN) and hemoglobins (HbCO, HbO2, and deoxyHb), as well as those of several mutants (W7F Mb, βW15F Hb, βW37S Hb, and βY130F Hb, all as the carbonmonoxy adducts), prepared via site-directed mutagenesis. The maximum observed chemical shift range induced by folding is 6.4 ppm. Using a multipole shielding polarizability−local reaction field approach, we have computed the electrostatic field contributions to the fluorine shielding. For residues which do not have F atoms in contact with neighboring groups, we find an ∼1 ppm mean square deviation in shift from experiment, with the R2-like structure of HbCOA being in very close accord with experiment.