Pulse Radiolysis Study of Catalytic Properties of Human Manganese Superoxide Dismutase: A Review
The depletion of superoxide catalyzed by human manganese superoxide dismutase (MnSOD) was observed spectrophotometrically by measuring the absorbance of superoxide at 250-280 nm following pulse radiolysis and it showed a biphasic pattern. Tryptophan 161 is a highly conserved residue that forms a hyd...
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| Main Author: | |
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| Format: | Article |
| Language: | English |
| Published: |
Hammer Head Production Limited
2016-07-01
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| Series: | Sokoto Journal of Medical Laboratory Science |
| Subjects: | |
| Online Access: | https://sokjmls.com.ng/index.php/SJMLS/article/view/369 |
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| Summary: | The depletion of superoxide catalyzed by human manganese superoxide dismutase (MnSOD) was observed spectrophotometrically by measuring the absorbance of superoxide at 250-280 nm following pulse radiolysis and it showed a biphasic pattern. Tryptophan 161 is a highly conserved residue that forms a hydrophobic side of the active site cavity of manganese superoxide dismutase (MnSOD), with its indole ring adjacent to and about 5 Å from the manganese. Trp 161 promotes the dissociation of product peroxide, perhaps in part through its effect on the orientation of Tyr 34. |
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| ISSN: | 2536-7153 |