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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.
- 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