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

Detcho A. Stoyanovsky; Alexandr Kapralov; Zhentai Huang; Akihiro Maeda; Anatoly Osipov; Carleton J.C. Hsia; Li Ma; Patrick M. Kochanek; Hulya Bayr; Valerian E. Kagan

doi:10.1016/j.bbrc.2010.07.030

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

Detcho A. Stoyanovsky, Alexandr Kapralov, Zhentai Huang, Akihiro Maeda, Anatoly Osipov, Carleton J.C. Hsia, Li Ma, Patrick M. Kochanek, Hulya Bayr, Valerian E. Kagan

Biochemistry, Chemistry, & Physics

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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)₁₂ exhibits 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.

Original language	American English
Journal	Biochemical and Biophysical Research Communications
Volume	399
DOIs	https://doi.org/10.1016/j.bbrc.2010.07.030
State	Published - Aug 20 2010

Keywords

H2O2
Hemoglobin
Nitroxide
Peroxidase

DC Disciplines

Physics

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http://dx.doi.org/10.1016/j.bbrc.2010.07.030

Cite this

Stoyanovsky, D. A., Kapralov, A., Huang, Z., Maeda, A., Osipov, A., Hsia, C. J. C., Ma, L., Kochanek, P. M., Bayr, H., & Kagan, V. E. (2010). Unusual Peroxidase Activity of Polynitroxylated Pegylated Hemoglobin: Elimination of H₂O₂ Coupled with Intramolecular Oxidation of Nitroxides. Biochemical and Biophysical Research Communications, 399. https://doi.org/10.1016/j.bbrc.2010.07.030

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title = "Unusual Peroxidase Activity of Polynitroxylated Pegylated Hemoglobin: Elimination of H2O2 Coupled with Intramolecular Oxidation of Nitroxides",

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)12 exhibits 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.",

keywords = "H2O2, Hemoglobin, Nitroxide, Peroxidase",

author = "Stoyanovsky, {Detcho A.} and Alexandr Kapralov and Zhentai Huang and Akihiro Maeda and Anatoly Osipov and Hsia, {Carleton J.C.} and Li Ma and Kochanek, {Patrick M.} and Hulya Bayr and Kagan, {Valerian E.}",

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T1 - Unusual Peroxidase Activity of Polynitroxylated Pegylated Hemoglobin: Elimination of H2O2 Coupled with Intramolecular Oxidation of Nitroxides

AU - Stoyanovsky, Detcho A.

AU - Kapralov, Alexandr

AU - Huang, Zhentai

AU - Maeda, Akihiro

AU - Osipov, Anatoly

AU - Hsia, Carleton J.C.

AU - Ma, Li

AU - Kochanek, Patrick M.

AU - Bayr, Hulya

AU - Kagan, Valerian E.

PY - 2010/8/20

Y1 - 2010/8/20

N2 - 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)12 exhibits 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.

AB - 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)12 exhibits 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.

KW - H2O2

KW - Hemoglobin

KW - Nitroxide

KW - Peroxidase

UR - https://digitalcommons.georgiasouthern.edu/physics-facpubs/36

UR - http://dx.doi.org/10.1016/j.bbrc.2010.07.030

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DO - 10.1016/j.bbrc.2010.07.030

M3 - Article

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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