一种分析复杂体系 51V 固态 NMR 谱的简单方法。

A simple method for analyzing 51V solid-state NMR spectra of complex systems.

机构信息

Institut für Physikalische Chemie, Friedrich-Schiller-Universität Jena, Jena, Germany.

出版信息

Solid State Nucl Magn Reson. 2011 Sep;40(2):60-5. doi: 10.1016/j.ssnmr.2011.05.001. Epub 2011 May 14.

DOI:10.1016/j.ssnmr.2011.05.001

Abstract

Five vanadium complexes as models for biological systems were investigated using (51)V-MAS-NMR spectroscopy. All spectra show an uncommon line shape, which can be attributed to a shorter relaxation time of the satellite transition in contrast to the central one. A method for the reliable analysis of such kind of spectra is presented for the first time and the most important NMR parameters of the investigated complexes (quadrupolar coupling constant C(Q), asymmetry of the EFG tensor η(Q), isotropic chemical shift δ(iso), chemical shift anisotropy δ(σ) and asymmetry of the CSA tensor η(σ)) are presented. These results are of particular importance with respect to the analysis of the (51)V-MAS-NMR spectra of vanadium moieties in biological matrices such as vanadium chloroperoxidase, which show hitherto unexplained low intensity of the satellite sideband pattern.

摘要

使用 (51)V-MAS-NMR 光谱法研究了五种作为生物体系模型的钒配合物。所有光谱均显示出一种不常见的线形，这可以归因于卫星跃迁的弛豫时间相对于中心跃迁较短。首次提出了一种用于可靠分析此类光谱的方法，并给出了所研究配合物的最重要的 NMR 参数（四极耦合常数 C(Q)、EFG 张量不对称性 η(Q)、各向同性化学位移 δ(iso)、化学位移各向异性 δ(σ) 和 CSA 张量不对称性 η(σ))。这些结果对于分析生物基质中的钒部分的 (51)V-MAS-NMR 光谱特别重要，例如钒氯过氧化物酶，其卫星边带模式的强度迄今仍未得到解释。