The Contribution of the α and β Chains to the Kinetics of Oxygen Binding to and Dissociation from Hemoglobin
The Contribution of the α and β Chains to the Kinetics of Oxygen Binding to and Dissociation from Hemoglobin
复制标题
α 链和 β 链对氧与血红蛋白结合和解离动力学的贡献
DOI：
--
复制
发表时间：
1973
期刊：
影响因子：
--
通讯作者：
Q. Gibson
中科院分区：
文献类型：
--
作者：
Q. Gibson
一种新的实验表明，将血红蛋白短暂地暴露在氧气中，氧从某些部分氧化的中间体中解离的半衰期在20°下约为1毫秒，在2°下约为10毫秒。快速解离选择性地发生在一种类型的链上，暂时被鉴定为β链。显示出快速分解氧的链也快速结合。因此，动力学等效的Adair方程和Monod-Wyman-Changeux模型是非常不适合代表氧-血红蛋白反应的动力学。氧与血红蛋白的反应与烷基异氰化物的反应非常相似，而与一氧化碳的反应截然不同。
A new type of experiment in which hemoglobin is exposed briefly to oxygen has shown that the half-time of dissociation of oxygen from some partly oxygenated intermediates is about 1 msec at 20° and 10 msec at 2°. The rapid dissociation occurs selectively from one type of chain, provisionally identified as the β-chain. Chains that show the rapid rate of dissociation of oxygen also bind rapidly. It follows that the kinetic equivalent of the Adair equation and the Monod-Wyman-Changeux model are quite unsuited to represent the kinetics of the oxygen-hemoglobin reaction. The reaction of oxygen with hemoglobin closely resembles that of the alkyl isocyanides and differs radically from that of carbon monoxide.