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

Gayathri      Vasudevan; Melisenda   J.   McDonald

doi:10.2174/1389203023380602

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 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.

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

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Current Protein & Peptide Science

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

Volume: 3 Issue: 4

Author(s): Gayathri Vasudevan and Melisenda J. McDonald

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

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 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.

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Vasudevan Gayathri and McDonald J. Melisenda, Ordered Heme Binding Ensures the Assembly of Fully Functional Hemoglobin: A Hypothesis, Current Protein & Peptide Science 2002; 3 (4) . https://dx.doi.org/10.2174/1389203023380602