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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Recombinant hemoglobins with low oxygen affinity and high cooperativity.
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Recombinant hemoglobins with low oxygen affinity and high cooperativity.

机译：具有低氧亲和力和高协同性的重组血红蛋白。

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摘要

By introducing an additional H-bond in the alpha(1)beta(2) subunit interface or altering the charge properties of the amino acid residues in the alpha(1)beta(1) subunit interface of the hemoglobin molecule, we have designed and expressed recombinant hemoglobins (rHbs) with low oxygen affinity and high cooperativity. Oxygen-binding measurements of these rHbs under various experimental conditions show interesting properties in response to pH (Bohr effect) and allosteric effectors. Proton nuclear magnetic resonance studies show that these rHbs can switch from the oxy (or CO) quaternary structure (R) to the deoxy quaternary structure (T) without changing their ligation states upon addition of an allosteric effector, inositol hexaphosphate, and/or reduction of the ambient temperature. These results indicate that if we can provide extra stability to the T state of the hemoglobin molecule without perturbing its R state, we can produce hemoglobins with low oxygen affinity and high cooperativity. Some of these rHbs are also quite stable against autoxidation compared to many of the known abnormal hemoglobins with altered oxygen affinity and cooperativity. These results have provided new insights into the structure-function relationship in hemoglobin.
机译：通过在alpha（1）beta（2）亚基界面中引入额外的H键或改变血红蛋白分子alpha（1）beta（1）亚基界面中氨基酸残基的电荷性质，我们设计并表达的重组血红蛋白（rHbs）具有低氧亲和力和高协同性。在各种实验条件下对这些rHb的氧结合测量显示出对pH值（玻尔效应）和变构效应物感兴趣的特性。质子核磁共振研究表明，这些rHb可以在添加变构效应物，六磷酸肌醇和/或还原后，从氧（或CO）四元结构（R）切换为脱氧四元结构（T）而不会改变其连接状态。环境温度这些结果表明，如果我们能够为血红蛋白分子的T状态提供额外的稳定性而不干扰其R状态，那么我们可以生产出具有低氧亲和力和高协同性的血红蛋白。与许多已知的异常血红蛋白相比，这些rHb中的一些还具有很好的抗自氧化性，并且氧亲和力和协同性发生了变化。这些结果为血红蛋白的结构-功能关系提供了新的见解。

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