Unusual Peroxidase Activity of Polynitroxylated Pegylated Hemoglobin: Elimination of H(2)O(2) Coupled with Intramolecular Oxidation of Nitroxides
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2010/08/20
Details
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Personal Author:Bayr H ; Hsia CJC ; Huang Z ; Kagan VE ; Kapralov A ; Kochanek PM ; Ma L ; Maeda A ; Osipov A ; Stoyanovsky DA
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Description: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. [Description provided by NIOSH]
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ISSN:0006-291X
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Pages in Document:139-143
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Volume:399
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Issue:2
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NIOSHTIC Number:nn:20037617
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Citation:Biochem Biophys Res Commun 2010 Aug; 399(2):139-143
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Contact Point Address:Valerian E. Kagan, Department of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA 15219
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Email:kagan@pitt.edu
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Federal Fiscal Year:2010
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Performing Organization:University of Pittsburgh at Pittsburgh
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Peer Reviewed:True
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Start Date:20050701
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Source Full Name:Biochemical and Biophysical Research Communications
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End Date:20160630
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Main Document Checksum:urn:sha-512:d0cf60957caa1fb7a42763cda3e4021d6179ab89e6c8b895c145a2f720209f79a4f6225268fe9041a03a8fb6037ce5b67c688c39a082b33f6e2bbc4bccca83bf
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