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首页> 外文期刊>The journal of physical chemistry, A. Molecules, spectroscopy, kinetics, environment, & general theory >Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins
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Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

机译：金属蛋白的非常低频宽带电子顺磁共振谱谱

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摘要

A previously developed spectrometer for broadband electron paramagnetic resonance (EPR) spectroscopy of dilute randomly oriented systems has been considerably modified to extend the frequency reach down to the hundred MHz range and to boost concentration sensitivity by 1 to 2 orders of magnitude. The instrument is now suitable for the study of biological systems in particular metalloproteins. As a proof of concept, examples from the class of low-spin ferric hemoproteins are studied in terms of frequency-dependent changes in their EPR spectra. Mono-heme cytochrome c EPR is determined by g-strain over a wide frequency range, whereas a combination of unresolved ligand hyperfine interaction and concentration-dependent intermolecular dipolar interaction becomes dominant at very low frequencies. In the four heme containing cytochrome c(3), g-strain combines with intramolecular dipolar interaction over the full-studied frequency range of 0.23-12.0 GHz. It is concluded that the point-dipole approach is inappropriate to describe magnetic interactions between low-spin ferric heme systems and that a body of literature on redox interactions in multi-heme proteins will be affected by this conclusion.
机译：先前开发的用于稀释随机取向系统的宽带电子顺磁共振（EPR）光谱的光谱仪已经进行了相当大的修改，以将频率范围扩展到100 MHz范围，并将浓度灵敏度提高1到2个数量级。该仪器现在适用于研究生物系统，尤其是金属蛋白。作为概念证明，我们根据低自旋铁血蛋白的EPR谱的频率依赖性变化研究了这类血蛋白的例子。单血红素细胞色素c EPR由g-应变在很宽的频率范围内确定，而在非常低的频率下，未解决的配体超精细相互作用和浓度依赖的分子间偶极相互作用的组合占主导地位。在四种含血红素的细胞色素c（3）中，g-菌株在0.23-12.0 GHz的整个研究频率范围内与分子内偶极相互作用结合。结论是，点偶极子方法不适合描述低自旋铁血红素系统之间的磁相互作用，并且多血红素蛋白质中氧化还原相互作用的大量文献将受到这一结论的影响。

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