Reaction of hemoglobin with HOCl: mechanism of heme destruction and free iron release.

@article{Maitra2011ReactionOH,
  title={Reaction of hemoglobin with HOCl: mechanism of heme destruction and free iron release.},
  author={Dhiman Maitra and Jaeman Byun and Peter R Andreana and Ibrahim Abdulhamid and Michael Peter Diamond and Ghassan M. Saed and Subramaniam Pennathur and Husam M Abu-Soud},
  journal={Free radical biology & medicine},
  year={2011},
  volume={51 2},
  pages={374-86}
}
Hypochlorous acid (HOCl) is generated by myeloperoxidase using chloride and hydrogen peroxide as substrates. HOCl and its conjugate base (OCl(-)) bind to the heme moiety of hemoglobin (Hb) and generate a transient ferric species whose formation and decay kinetics indicate it can participate in protein aggregation and heme destruction along with subsequent free iron release. The oxidation of the Hb heme moiety by OCl(-) was accompanied by marked heme destruction as judged by the decrease in and… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 16 extracted citations

Similar Papers

Loading similar papers…