Synthesis of Polymeric Reconstituted Hemoglobins as Superoxide Dismutase Mimics Designed for Long-term Circulation Maintenance

Makoto Yuasa, Kenichi Oyaizu, Takamitsu Hayashi, Aritomo Yamaguchi

Research output: Contribution to journalArticle

3 Citations (Scopus)


Superoxide dismutase (SOD), catalase and glutathione peroxidase catalize the elimination of reactive oxygen species (ROS) such as a superoxide anion radical (O2-·). But enzyme activity decreases in diseases in which ROS attacks DNA, lipid and blood vessels. Recent studies on SOD mimics indicate that manganese porphyrin (MnT2MePyP) express high SOD activity. But the half-life of MnT2MePyP in the blood is usually very short. In the present study, a novel reconstituted polymerized hemoglobin containing manganese porphyrins (MnT2MePyP-PolyHb) was synthesized. SOD activity of MnT2MePyP-PolyHb (IC50 = 1.1 μM, kcat = 7.3 × 106 M-1s-1) was found to be somewhat less than that of MnT2MePyP (IC50 = 0.23 μM, kcat = 60 × 106 M-1s-1). MnT2MePyP-PolyHb half-life in H2O2 (t1/2 = 1070 s) was found to be as much as four times that of MnT2MePyP (t1/2 = 250 s). MnT2MePyP-PolyHb may thus be a valid SOD model for effectively maintaining and prolonging blood circulation.

Original languageEnglish
Pages (from-to)413-418
Number of pages6
JournalJournal of oleo science
Issue number7
Publication statusPublished - 2005 Jan 1



  • cationic metalloporphyrin
  • circuration persistence
  • polymerized hemoglobin
  • reconstituted hemoglobin
  • superoxide dismutase mimic

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this