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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Detalles Bibliográficos
Autores principales: Zhou, Danlei, Hemann, Craig, Boslett, James, Luo, Aiqin, Zweier, Jay L., Liu, Xiaoping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458454/
https://www.ncbi.nlm.nih.gov/pubmed/28593139
http://dx.doi.org/10.1002/2211-5463.12230

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458454/
https://www.ncbi.nlm.nih.gov/pubmed/28593139
http://dx.doi.org/10.1002/2211-5463.12230

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