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

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

Journal Name: Current Protein & Peptide Science

Volume 3 , Issue 4 , 2002

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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Article Details

VOLUME: 3
ISSUE: 4
Year: 2002
Page: [461 - 466]
Pages: 6
DOI: 10.2174/1389203023380602
Price: $58

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