Mims W B, Peisach J
Biochemistry. 1976 Aug 24;15(17):3863-9. doi: 10.1021/bi00662a033.
The electron spin echo decay envelope for the blue copper protein, stellacyanin, and for a number of other Cu(II) complexes has been studied. Particular attention was given to the form of the "nuclear modulation" patterns, which show the effects of coupling between the electron spin and the neighboring nuclei. The envelopes for the hydrated cupric complex and for copper(II) glycylglycine were essentially the same and indicative of the coupling to protons. The peptide complex contains nitrogen nuclei coupled directly to Cu(II), but the coupling constant is so large for these nuclei that a modulation pattern ascribable to 14N is not seen. For copper(II) bovine serum albumin, on the other hand, a contribution due to the coupling of the remote nitrogen belonging to a histidyl imidazole ligand was observed. The modulation pattern for this complex and for stellacyanin closely resembled one another, strongly suggesting that an imidazole is ligated to the copper in this blue protein.
对蓝铜蛋白、漆树蓝蛋白以及其他一些铜（II）配合物的电子自旋回波衰减包络进行了研究。特别关注了“核调制”模式的形式，该模式显示了电子自旋与相邻原子核之间耦合的影响。水合铜配合物和铜（II）甘氨酰甘氨酸的包络基本相同，表明与质子发生了耦合。肽配合物含有直接与铜（II）耦合的氮原子核，但这些原子核的耦合常数非常大，以至于看不到可归因于14N的调制模式。另一方面，对于铜（II）牛血清白蛋白，观察到了由于属于组氨酸咪唑配体的远程氮的耦合而产生的贡献。该配合物和漆树蓝蛋白的调制模式彼此非常相似，强烈表明在这种蓝色蛋白质中咪唑与铜相连。
