Assignment of protoheme Resonance Raman spectrum by heme labeling in myoglobin
Assignment of protoheme Resonance Raman spectrum by heme labeling in myoglobin
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DOI：
10.1021/ja962239e
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发表时间：
1996-12-18
影响因子：
15
通讯作者：
Spiro, TG
中科院分区：
文献类型：
--
作者：
Hu, SZ;Smith, KM;Spiro, TG
报告了用七种血红素同位素重构的肌红蛋白的共振拉曼 (RR) 光谱，这些同位素异构体在卟啉骨架或乙烯基和丙酸酯取代基上用 N-15 和内消旋 D-4 标记。根据观察到的同位素位移，将 RR 谱带分配给卟啉面内和面外模式以及取代基的内部振动。重新审视乙烯基取代基效应的问题，并通过选择性氘化位移将谱带分配给 2- 或 4- 乙烯基。 RR 光谱中还揭示了脂肪族丙酸酯基团的贡献。蛋白质对血红素结构的影响反映在低频区域中几种面外模式的激活。
Resonance Raman (RR) spectra are reported for myoglobin reconstituted with seven heme isotopomers which are labeled with N-15 and meso-D-4 in the porphyrin skeleton or at the vinyl and propionate substituents. The RR bands are assigned to the porphyrin in-plane and out-of-plane modes as well as to the internal vibrations of substituents on the basis of the observed isotope shifts. The issue of vinyl substituent effects is revisited, and bands are assigned to the 2- or 4-vinyl group from selective deuteration shifts. Contributions of the aliphatic propionate groups are also revealed in the RR spectrum. The protein influence on the heme structure is reflected in the activation of several out-of-plane modes in the low-frequency region.