The Generation of Superoxide Radical during the Autoxidation of Hemoglobin
Journal of Biological ChemistryPublished 1 November 1972Open access
Hara P. Misra, Irwin Fridovich
Citations1,171
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
Clostridial and spinach ferredoxins, reduced enzymatically by the action of ferredoxin-TPN+ oxidoreductase, have been shown to carry out the univalent reduction of oxygen.
Abstract
The autoxidation of oxyhemoglobin to methemoglobin, at pH 6.8, causes the co-oxidation of epinephrine to adrenochrome. Part of this co-oxidation was due to a hemoglobincatalyzed peroxidation of epinephrine and could be inhibited by catalase. The remainder of the co-oxidation of epinephrine was inhibited by superoxide dismutase. This indicates that the autoxidation of oxyhemoglobin results in the generation of superoxide radicals.
Keywords
Agricultural and Biological SciencesBiochemistry, Genetics and Molecular Biology
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