脱氧血红蛋白考伊敦[His HC3(146)β→Leu]的结构：血红蛋白中碱性玻尔效应和静电相互作用的起源
Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin.
作者信息
Perutz M F, Fermi G, Shih T B
出版信息
Proc Natl Acad Sci U S A. 1984 Aug;81(15):4781-4. doi: 10.1073/pnas.81.15.4781.
Abstract
Hemoglobin Cowtown [His HC3(146)-beta----Leu] exhibits high oxygen affinity and a halved alkaline Bohr effect. X-ray analysis shows the COOH-terminal leucine to be in equilibrium between two positions: one with the salt bridge between the terminal carboxyl and Lys C5(40)alpha intact and the leucyl side chain leaning against main chain atoms of helices F and FG and the other with the terminal salt bridge broken and the leucyl side chain touching Pro C2(37)alpha. Structural changes are confined to the immediate neighborhood of the COOH terminus, showing the halving of the alkaline Bohr effect to be due directly to the loss of the histidine, without significant contributions from changes in pK values of other ionizable groups due to structural changes elsewhere.
摘要
考恩镇血红蛋白[His HC3(146)-β----Leu]表现出高氧亲和力和减半的碱性玻尔效应。X射线分析表明，COOH末端的亮氨酸处于两个位置之间的平衡状态：一个位置是末端羧基与Lys C5(40)α之间的盐桥完整，亮氨酰侧链靠在螺旋F和FG的主链原子上；另一个位置是末端盐桥断裂，亮氨酰侧链与Pro C2(37)α接触。结构变化局限于COOH末端的紧邻区域，表明碱性玻尔效应减半直接归因于组氨酸的缺失，而不是由于其他地方结构变化导致的其他可电离基团pK值变化的显著贡献。
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