Faculty Collaboration Database

Hydrogen peroxide modification of human oxyhemoglobin. Free Radic Res Commun 1991;12-13 Pt 2:489-97

Date

01/01/1991

Pubmed ID

2060826

DOI

10.3109/10715769109145822

Scopus ID

2-s2.0-84907034319 (requires institutional sign-in at Scopus site)   13 Citations

Abstract

The effect of H2O2 on the primary structure of OxyHb was studied. Upon treatment of OxyHb with H2O2 ([Heme]/[H2O2] = 1), tryptophan and methionine residues of the beta-chain were modified. Treatment of ApoHb with H2O2 resulted in the modification of histidine and methionine residues in both globin chains. Tryptophan residues were unaffected. Modification of methionine residues in both the beta-chain of OxyHb and ApoHb probably results from the direct oxidation of methionine by H2O2. The modification of histidine residues in ApoHb may be mediated by a metal-catalyzed oxidation system comprised of H2O2 and histidine-bound iron. The H2O2-mediated modification of tryptophan in the OxyHb beta-chain, however, requires the heme moiety.

Author List

Steffek RP, Thomas MJ

MESH terms used to index this publication - Major topics in bold

Amino Acids
Apoproteins
Chromatography, High Pressure Liquid
Globins
Heme
Hemoglobin A
Hemoglobins
Humans
Hydrogen Peroxide
Iron
Oxyhemoglobins
Peptide Mapping
Trypsin