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T态血红蛋白中不存在血红素定位应变：血红素-咪唑共振拉曼频率对四级结构不敏感。

Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure.

作者信息

Kincaid J, Stein P, Spiro T G

出版信息

Proc Natl Acad Sci U S A. 1979 Feb;76(2):549-52. doi: 10.1073/pnas.76.2.549.

DOI:10.1073/pnas.76.2.549
PMID:284379
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC382985/
Abstract

Substitution of pentadeuterated 2-methylimidazole in (2-methylimidazole)-Fe(II)-protoporphyrin IX, a model complex for deoxyHb, shifts three bands in the low-frequency resonance Raman spectrum 380 leads to 373 cm-1, 348 leads to 345 cm-1, and 220 leads to 218 cm-1. The first of these is assigned primarily to Fe-imidazole stretching, and the other two are assigned to porphyrin deformation modes with substantial Fe-pyrrole stretching contributions. The three bands are observed in deoxyHb and Mb. The Fe-pyrrole modes are at essentially the same frequencies in the two proteins, but the Fe-imidazole mode is 6 cm-1 lower in deoxyHb than Mb, implying a slight alteration in the heme-imidazole linkage. No change greater than 2 cm-1 is observed when Hb Kempsey is switched from the R to the T state. This observation places an upper limit on the energy stored in the Fe-imidazole bond of T state deoxyHb, which is estimated to be less than 0.2 kcal/mol (less than 836.8 J/mol).

摘要

在作为脱氧血红蛋白模型配合物的（2-甲基咪唑）-铁（II）-原卟啉IX中，用五氘代2-甲基咪唑进行取代，使得低频共振拉曼光谱中的三条谱带发生位移，380 cm-1移至373 cm-1，348 cm-1移至345 cm-1，220 cm-1移至218 cm-1。其中第一条谱带主要归因于铁-咪唑伸缩振动，另外两条归因于具有大量铁-吡咯伸缩振动贡献的卟啉变形模式。这三条谱带在脱氧血红蛋白和肌红蛋白中都能观察到。两种蛋白质中铁-吡咯模式的频率基本相同，但脱氧血红蛋白中铁-咪唑模式的频率比肌红蛋白低6 cm-1，这意味着血红素-咪唑键存在轻微改变。当肯普西血红蛋白从R态转变为T态时，观察到的变化不超过2 cm-1。这一观察结果为T态脱氧血红蛋白中铁-咪唑键储存的能量设定了上限，估计该能量小于0.2千卡/摩尔（小于836.8焦耳/摩尔）。

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本文引用的文献

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Raman study on the two quaternary states of unligated hemoglobin.未结合配体血红蛋白两种四级状态的拉曼光谱研究。
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Resonance Raman spectra of liganded and unliganded carp hemoglobin in both R and T states.处于R态和T态的配位和未配位鲤鱼血红蛋白的共振拉曼光谱。
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