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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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Bibliographische Detailangaben
Veröffentlicht in:FEBS Open Bio
Hauptverfasser: Zhou, Danlei, Hemann, Craig, Boslett, James, Luo, Aiqin, Zweier, Jay L., Liu, Xiaoping
Format: Artigo
Sprache:Inglês
Veröffentlicht: John Wiley and Sons Inc. 2017
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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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