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J Biol Chem, Vol. 273, Issue 21, 13037-13046, May 22, 1998

Identification of a Nickel(II) Binding Site on Hemoglobin Which Confers Susceptibility to Oxidative Deamination and Intramolecular Cross-linking

From Somatogen Inc., Boulder, Colorado 80301

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 (Oxone^TM). Both the oxidative deamination and cross-linking are exclusive to the  chains. Recombinant hemoglobin mutants have been created to identify protein sequence requirements for these reactions. It was found that His-2 of the  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  chain. Most cross-linking of the  globin occurs intramolecularly, forming  globin dimers. Structural characterization of the  globin dimers indicates the presence of heterogeneous cross-links within the central hemoglobin cavity between the NH₂ terminus of one  chain and the COOH-terminal region of the other.

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				J. Levine, J. Etter, and I. Apostol Nickel-catalyzed N-terminal Oxidative Deamination in Peptides Containing Histidine at Position 2 Coupled with Sulfite Oxidation J. Biol. Chem., February 19, 1999; 274(8): 4848 - 4857. [Abstract] [Full Text] [PDF]