Unusual Peroxidase Activity of Polynitroxylated Pegylated Hemoglobin: Elimination of H2O2 Coupled with Intramolecular Oxidation of Nitroxides

Document Type

Article

Publication Date

8-20-2010

Publication Title

Biochemical and Biophysical Research Communications

DOI

10.1016/j.bbrc.2010.07.030

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.

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