Department of Chemistry, University of York, York YO10 5YW, UK.
Biopolymers. 2009 Dec;91(12):1056-63. doi: 10.1002/bip.21197.
The two hemoglobin structures determined by Max Perutz, the liganded R-state, which has high oxygen affinity, and the unliganded T-state with low oxygen affinity, were landmarks in molecular and structural biology (Perutz and Lehman, Nature 1968, 219, 902-909; Bolton and Perutz, Nature 1970, 28, 551-552; Perutz et al., Nature 1968, 219, 131-139). They provided the basis of a structural mechanism that connected beautifully to the theory of cooperativity in protein systems, formulated at about the same time by Monod et al. (J Mol Biol 1965, 12, 88-1118). Over the last 40 years there have been extensive biochemical and structural studies on hemoglobin's structure and the mechanisms that govern its co-operativity, specificity, and other physiological properties. There are still however a number of unresolved issues over the molecule's properties, for example the mechanism responsible for the affects of pH on oxygen affinity, i.e., the Bohr and Root effects. In this communication the differences in the geometry at the a-heme of unliganded and liganded human and the Antarctic fish (Trematomus) hemoglobin will be described and their relevance to affinity considered.
由马克斯·佩鲁茨（Max Perutz）确定的两种血红蛋白结构，分别是配体结合的 R 态（具有高氧亲和力）和无配体结合的 T 态（具有低氧亲和力），这是分子和结构生物学的里程碑（佩鲁茨和莱曼，《自然》1968 年，219，902-909；博尔顿和佩鲁茨，《自然》1970 年，28，551-552；佩鲁茨等人，《自然》1968 年，219，131-139）。它们为连接蛋白质系统协同作用理论的结构机制提供了基础，这一理论是由莫诺等人在同一时期提出的（J Mol Biol 1965 年，12，88-1118）。在过去的 40 年里，人们对血红蛋白的结构及其协同作用、特异性和其他生理特性的机制进行了广泛的生化和结构研究。然而，对于该分子的特性，仍然存在一些尚未解决的问题，例如负责 pH 值对氧亲和力影响的机制，即 Bohr 和 Root 效应。在本通讯中，将描述无配体结合和配体结合的人类和南极鱼（ Trematomus ）血红蛋白的 a-血红素几何形状的差异，并考虑其对亲和力的相关性。
