Vasudevan Gayathri, McDonald Melisenda J
Department of Chemistry, University of Massachusetts, Lowell, 01854-5047, USA.
Curr Protein Pept Sci. 2002 Aug;3(4):461-6. doi: 10.2174/1389203023380602.
The exact mechanism by which four Fe-Protoporphyrin-IX (heme) moieties and four nascent globin chains combine to form human hemoglobin (alpha(2)beta(2)) remains a mystery. Recent Soret spectral static and kinetic studies of the incorporation of CN-Hemin derivatives into an array of human globin species have provided in vitro evidence of an ordered assembly pathway, through an alphaheme-betaglobin intermediate, that ensures correct formation of active hemoglobin tetramers.
四个亚铁原卟啉-IX（血红素）部分与四条新生的珠蛋白链结合形成人血红蛋白（α(2)β(2)）的确切机制仍是一个谜。最近，对氰化高铁血红素衍生物掺入一系列人珠蛋白种类的索雷特光谱静态和动力学研究提供了体外证据，证明存在一条有序的组装途径，该途径通过α-血红素-β-珠蛋白中间体确保活性血红蛋白四聚体的正确形成。
