通过共振拉曼光谱法观察高铁肌红蛋白的FeIV=O伸缩振动。
Observation of the FeIV=O stretching vibration of ferryl myoglobin by resonance Raman spectroscopy.
作者信息
Sitter A J, Reczek C M, Terner J
出版信息
Biochim Biophys Acta. 1985 Apr 29;828(3):229-35. doi: 10.1016/0167-4838(85)90301-2.
We have directly observed the oxyferryl group of ferryl myoglobin by resonance Raman spectroscopy. The FeIV = O stretching vibration is observed at 797 cm-1 and confirmed by an 18O-induced isotopic shift to 771 cm-1. The porphyrin center-to-nitrogen distance of ferryl myoglobin is significantly less than that previously observed for horseradish peroxidase compound II, which also contains an FeIV = O heme. The FeIII-CN- stretch of myoglobin (FeIII) cyanide is observed at 454 cm-1, which shifts to 449 cm-1 upon substitution with [13C]cyanide.
我们通过共振拉曼光谱法直接观察到了高铁肌红蛋白的氧合铁基团。在797厘米-1处观察到FeIV = O伸缩振动，并通过18O诱导的同位素位移证实其移至771厘米-1。高铁肌红蛋白的卟啉中心到氮的距离明显小于先前观察到的辣根过氧化物酶化合物II的距离，后者也含有一个FeIV = O血红素。肌红蛋白（FeIII）氰化物的FeIII-CN-伸缩在454厘米-1处观察到，在用[13C]氰化物取代后移至449厘米-1。
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