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Resonance Raman Spectra of Cobalt-Substituted Hemoglobin: Cooperativity and Displacement of the Cobalt Atom upon Oxygenation

机译:钴取代的血红蛋白的共振拉曼光谱:氧合作用和钴原子的置换

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摘要

The resonance Raman spectra of oxy and deoxy cobalt-substituted hemoglobin (CoHb) are reported. Comparison of these spectra to those of hemoglobin, methemoglobin, cytochrome c, and model cobalt porphyrin complexes suggests that the displacement of the cobalt atom upon oxygenation of CoHb is no greater than the out-of-plane distance in five-coordinate Co(II) porphyrins, 0.15 Å. Combining this distance with the expected contraction of the cobalt-histidine bond, Ibers has estimated a maximum displacement of 0.37 Å for the proximal histidine with respect to the heme plane upon oxygenation, about one-third the corresponding distance estimated for iron hemoglobin. The free energy of cooperativity for cobalt hemoglobin is also estimated to be one-third that of iron hemoglobin. These results are therefore consistent with Hopfield's distributed energy model, which predicts proportionality between proximal histidine displacement and the free energy of cooperativity. By implication they support Perutz's trigger mechanism for cooperativity.
机译:报道了氧和脱氧钴取代的血红蛋白(CoHb)的共振拉曼光谱。这些光谱与血红蛋白,高铁血红蛋白,细胞色素c和模型钴卟啉配合物的光谱比较表明,CoHb氧化后钴原子的位移不大于五坐标Co(II)中的平面外距离卟啉,0.15Å。将这个距离与钴-组氨酸键的预期收缩结合在一起,Ibers估计,在氧合时,近端组氨酸相对于血红素平面的最大位移为0.37埃,约为铁血红蛋白估算距离的三分之一。钴血红蛋白的协同作用自由能也估计为铁血红蛋白的自由能的三分之一。因此,这些结果与Hopfield的分布式能量模型相一致,该模型预测了近端组氨酸的位移与合作性自由能之间的比例。这暗示着他们支持佩鲁茨的合作触发机制。

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