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Oxygen binding and nitric oxide dioxygenase activity of cytoglobin are altered to different extents by cysteine modification
Cytoglobin (Cygb), like other members of the globin family, is a nitric oxide (NO) dioxygenase, metabolizing NO in an oxygen (O(2))‐dependent manner. We examined the effect of modification of cysteine sulfhydryl groups of Cygb on its O(2) binding and NO dioxygenase activity. The two cysteine sulfhyd...
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| Veröffentlicht in: | FEBS Open Bio |
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| Hauptverfasser: | , , , , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
John Wiley and Sons Inc.
2017
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5458454/ https://ncbi.nlm.nih.gov/pubmed/28593139 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/2211-5463.12230 |
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