Title: Ordered Heme Binding Ensures the Assembly of Fully Functional Hemoglobin: A Hypothesis
Abstract:The exact mechanism by which four Fe-Protoporphyrin-IX (heme) moieties and four nascent globin chains combine to form human hemoglobin (α2β2) remains a mystery. Recent Soret spectral static and kineti...The exact mechanism by which four Fe-Protoporphyrin-IX (heme) moieties and four nascent globin chains combine to form human hemoglobin (α2β2) 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 αheme-βglobin intermediate, that ensures correct formation of active hemoglobin tetramers.Read More
Publication Year: 2002
Publication Date: 2002-08-01
Language: en
Type: review
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 10
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