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PubMed · 12370008

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

Gayathri Vasudevan·Melisenda J McDonald
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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.

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HemeHemoglobinsHumansKineticsProtein BindingProtein Processing, Post-TranslationalProtein Structure, QuaternaryProtein SubunitsJournal ArticleResearch Support, Non-U.S. Gov'tReview

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Gayathri Vasudevan, Melisenda J McDonald. 2002. Ordered heme binding ensures the assembly of fully functional hemoglobin: a hypothesis.. https://doi.org/10.2174/1389203023380602

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