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Unusual peroxidase activity of polynitroxylated pegylated hemoglobin: elimination of H(2)O(2) coupled with intramolecular oxidation of nitroxides.

Authors
Stoyanovsky-DA; Kapralov-A; Huang-Z; Maeda-A; Osipov-A; Hsia-CJC; Ma-L; Kochanek-PM; Bayr-H; Kagan-VE
Source
Biochem Biophys Res Commun 2010 Aug; 399(2):139-143
NIOSHTIC No.
20037617
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 H(2)O(2) is utilized for intramolecular oxidation of its TPOH residues to TPO. This represents an unusual redox-catalytic mechanism whereby reduction of H(2)O(2) 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
Biological-effects; Blood-analysis; Blood-cells; Blood-serum; Blood-stream; Catalysis; Cell-biology; Cell-damage; Cell-function; Cellular-reactions; Hydroxylation-reactions; Microbiology; Microscopic-analysis; Molecular-biology; Molecular-structure; Oxidation; Oxidation-reduction-reactions; Oxidative-processes; Oxygen-transport; Plasma-membrane; Author Keywords: Hemoglobin; H2O2; Peroxidase; Nitroxide
Contact
Valerian E. Kagan, Department of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA 15219
CODEN
BBRCA9
Publication Date
20100820
Document Type
Journal Article
Email Address
kagan@pitt.edu
Funding Type
Grant
Fiscal Year
2010
NTIS Accession No.
NTIS Price
Identifying No.
Grant-Number-R01-OH-008282
Issue of Publication
2
ISSN
0006-291X
Source Name
Biochemical and Biophysical Research Communications
State
WV; PA; GA; CA
Performing Organization
University of Pittsburgh at Pittsburgh
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