| Autor: |
Levine, J, Weickert, M, Pagratis, M, Etter, J, Mathews, A, Fattor, T, Lippincott, J, Apostol, I |
| Zdroj: |
Journal of Biological Chemistry; May 1998, Vol. 273 Issue: 21 p13037-46, 10p |
| Abstrakt: |
Complexation of Ni(II) with native state recombinant hemoglobin is shown to produce NH2-terminal deamination and globin cross-linking in the presence of the oxidant potassium peroxymonosulfate (OxoneTM). Both the oxidative deamination and cross-linking are exclusive to the beta chains. Recombinant hemoglobin mutants have been created to identify protein sequence requirements for these reactions. It was found that His-2 of the beta globin is required for redox active Ni(II) complexation, oxidative deamination, and cross-linking. The oxidative deamination results in the formation of a free carbonyl in place of the NH2-terminal amine of the beta chain. Most cross-linking of the beta globin occurs intramolecularly, forming beta globin dimers. Structural characterization of the beta globin dimers indicates the presence of heterogeneous cross-links within the central hemoglobin cavity between the NH2 terminus of one beta chain and the COOH-terminal region of the other. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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