Resonance Raman scattering studies of the quaternary structure transition in hemoglobin.
Resonance Raman scattering studies of the quaternary structure transition in hemoglobin.
复制标题
血红蛋白四级结构转变的共振拉曼散射研究。
DOI：
10.1146/annurev.bb.12.060183.002041
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
M. Ondrias
中科院分区：
文献类型：
--
作者：
D. Rousseau;M. Ondrias
尽管经过多年的研究，血红蛋白（Hb）协同作用的分子机制仍未得到很好的理解。目前尚不清楚，在高亲和和低亲和形式的蛋白质中，氧结合的“，4千卡差异是由于定位于少数键（可能在血红素上）的相互作用，还是由于在许多键上的相互作用。事实上，直到最近才检测到血红素中详细的四元结构引起的变化（45）。此外，一个血红素位点上的配体结合信息传递到其他位点的途径尚未被发现。由于氧结合能差，即协同性的自由能，是一种热力学性质，它的位置可以通过检查脱氧和配体蛋白的高亲和力(R)和低亲和力(T)结构来确定（25）。评估这四种稳态蛋白质结构之间的能量差异应该能阐明哪些相互作用包含合作的自由能。共振拉曼散射在确定这些相互作用中起着非常重要的作用，因为它是涉及血红素基团的键的非常敏感的探针。
Despite many years of study, the molecular mechanism of cooperativity in hemoglobin (Hb) is not well understood. It is not known if the ",4 kcal difference for binding of O2 in the high affinity and low affinity forms of the protein results from interactions localized in a few bonds, possibly at the heme, or if it results from interactions delocalized over many bonds. Indeed, only recently have detailed quaternary structure-induced changes in the hemes been detected (45). Furthermore, the pathways by which information about ligand binding on one heme site is transmitted to the others has not been uncovered. Since the oxygen-binding energy difference, the free energy of cooperativity, is a thermodynamic property, its location can be determined from an examination of the deoxygenated and liganded proteins in both their high affinity (R) and low affinity (T) structures (25). An assessment of the energetic differences between these four steady-state protein structures should elucidate which interactions contain the free energy of cooperativity. Resonance Raman scattering plays a very import ant role in determining these interactions, since it is a very sensitive probe of the bonds involving the heme group.