亚铁血红素蛋白的 1H 和 13C 化学位移与模型亚铁血红素之间的线性相关关系。
Linear correlation between 1H and 13C chemical shifts of ferriheme proteins and model ferrihemes.
机构信息
Department of Chemistry and Biochemistry, The University of Arizona, P.O. Box 210041, Tucson, Arizona 85721-0041, United States.
出版信息
Inorg Chem. 2011 Feb 21;50(4):1176-83. doi: 10.1021/ic1020274. Epub 2011 Jan 18.
Abstract
The (1)H{(13)C} HMQC experiment at natural-abundance (13)C provides a very useful way of determining not only (1)H but also (13)C chemical shifts of most heme substituents, without isotopic labeling of the hemin. This is true both in model low-spin ferriheme complexes and in low-spin ferriheme proteins, even when the proton resonances are buried in the protein diamagnetic region, because the carbon shifts are much larger than the proton shifts. In addition, in many cases, the protohemin methyl cross peaks are fairly linearly related to each other, with the slope of the correlation, δ(C)/δ(H), being approximately -2.0 for most low-spin ferriheme proteins. The reasons why this should be the case, and when it is not, are discussed.
摘要
天然丰度 (13)C 的 (1)H{(13)C} HMQC 实验提供了一种非常有用的方法，不仅可以确定 (1)H 化学位移，还可以确定大多数血红素取代基的 (13)C 化学位移，而无需对血红素进行同位素标记。这在模型低自旋亚铁血红素配合物和低自旋亚铁血红素蛋白中都是如此，即使质子共振被埋藏在蛋白质抗磁性区域中，因为碳位移比质子位移大得多。此外，在许多情况下，原血红素甲基交叉峰彼此之间呈相当线性的关系，相关的斜率 δ(C)/δ(H) 对于大多数低自旋亚铁血红素蛋白来说约为-2.0。讨论了为什么会这样，以及什么时候不会这样的原因。
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