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Unusual Peroxidase Activity of Polynitroxylated Pegylated Hemoglobin: Elimination of H2O2 Coupled with Intramolecular Oxidation of Nitroxides
Biochemical and Biophysical Research Communications
  • Detcho A. Stoyanovsky, University of Pittsburgh
  • Alexandr Kapralov, University of Pittsburgh
  • Zhentai Huang, University of Pittsburgh
  • Akihiro Maeda, University of Pittsburgh
  • Anatoly Osipov, Russian State Medical University
  • Carleton J. C. Hsia, SynZyme Technologies, LLC
  • Li Ma, Georgia Southern University
  • Patrick M. Kochanek, University of Pittsburgh
  • Hülya Bayır, University of Pittsburgh
  • Valerian E. Kagan, University of Pittsburgh
Document Type
Article
Publication Date
8-20-2010
DOI
10.1016/j.bbrc.2010.07.030
Disciplines
Abstract

Polynitroxylated hemoglobin (Hb(AcTPO)12) has been developed as a hemoglobin-based oxygen carrier. While Hb(AcTPO)12 has been shown to exert beneficial effects in a number of models of oxidative injury, its peroxidase activity has not been characterized thus far. In the blood stream, Hb(AcTPO)12 undergoes reduction by ascorbate to its hydroxylamine form Hb(AcTPOH)12. Here we report that Hb(AcTPOH)12exhibits peroxidase activity where H2O2 is utilized for intramolecular oxidation of its TPOH residues to TPO. This represents an unusual redox-catalytic mechanism whereby reduction of H2O2 is achieved at the expense of reducing equivalents of ascorbate converted into those of Hb(AcTPOH)12, a new propensity that cannot be directly associated with ascorbate.

Citation Information
Detcho A. Stoyanovsky, Alexandr Kapralov, Zhentai Huang, Akihiro Maeda, et al.. "Unusual Peroxidase Activity of Polynitroxylated Pegylated Hemoglobin: Elimination of H2O2 Coupled with Intramolecular Oxidation of Nitroxides" Biochemical and Biophysical Research Communications Vol. 399 Iss. 2 (2010) p. 139 - 143
Available at: http://works.bepress.com/li_ma/33/