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Ordered Heme Binding Ensures the Assembly of Fully Functional Hemoglobin: A Hypothesis

[ Vol. 3 , Issue. 4 ]


Gayathri Vasudevan and Melisenda J. McDonald   Pages 461 - 466 ( 6 )


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.


Hemoglobin, Fe-Protoporphyrin-IX, CN-Hemin derivatives, aheme-bglobin


Department of Chemistry,University of Massachusetts, Lowell MA 01854-5047, USA

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