Ordered heme binding ensures the assembly of fully functional hemoglobin: a hypothesis.
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.
Vasudevan
Gayathri
G
Department of Chemistry, University of Massachusetts, Lowell, 01854-5047, USA.
McDonald
Melisenda J
MJ
D006418:Heme / Q000378:metabolism*; D006454:Hemoglobins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D020836:Protein Structure, Quaternary; D021122:Protein Subunits
D006454:Hemoglobins; D021122:Protein Subunits; D006418:Heme