A pulse radiolysis investigation of the reactions of myeloperoxidase with superoxide and hydrogen peroxide
Using pulse radiolysis, the rate constant for the reaction of ferric myeloperoxidase with O 2 − to give compound III was measured at pH 7.8, and values of 2.1 · 10 6 M −1 · s −1 for equine ferric myeloperoxidase and 1.1 · 10 6 M −1 · s −1 for human ferric myeloperoxidase were obtained. Under the sam...
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Published in | Biochimica et biophysica acta Vol. 956; no. 1; pp. 58 - 62 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
31.08.1988
Elsevier North-Holland |
Subjects | |
Online Access | Get full text |
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Summary: | Using pulse radiolysis, the rate constant for the reaction of ferric myeloperoxidase with O
2
− to give compound III was measured at pH 7.8, and values of 2.1 · 10
6 M
−1 · s
−1 for equine ferric myeloperoxidase and 1.1 · 10
6 M
−1 · s
−1 for human ferric myeloperoxidase were obtained. Under the same conditions, the rate constant for the reaction of human ferric myeloperoxidase with H
2O
2 to give compound I was 3.1 · 10
7 M
−1 · s
−1. Our results indicate that although the reaction of ferric myeloperoxidase with O
2
− is an order of magnitude slower than with H
2O
2, the former reaction is sufficiently rapid to influence myeloperoxidase-dependent production of hypochlorous acid by stimulated neutrophils. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0167-4838 0006-3002 1879-2588 1878-2434 |
DOI: | 10.1016/0167-4838(88)90297-X |