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Ordered heme binding ensures the assembly of fully functional hemoglobin: a hypothesis.

Ordered heme binding ensures the assembly of fully functional hemoglobin: a hypothesis.

Authors :
Vasudevan G
McDonald MJ
Source :
Current protein & peptide science [Curr Protein Pept Sci] 2002 Aug; Vol. 3 (4), pp. 461-6.
Publication Year :
2002

Abstract

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.

Details

Language :
English
ISSN :
1389-2037
Volume :
3
Issue :
4
Database :
MEDLINE
Journal :
Current protein & peptide science
Publication Type :
Academic Journal
Accession number :
12370008
Full Text :
https://doi.org/10.2174/1389203023380602