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The Single-domain Globin from the Pathogenic Bacterium Campylobacter jejuni: NOVEL D-HELIX CONFORMATION, PROXIMAL HYDROGEN BONDING THAT INFLUENCES LIGAND BINDING, AND PEROXIDASE-LIKE REDOX PROPERTIES
The food-borne pathogen Campylobacter jejuni possesses a single-domain globin (Cgb) whose role in detoxifying nitric oxide has been unequivocally demonstrated through genetic and molecular approaches. The x-ray structure of cyanide-bound Cgb has been solved to a resolution of 1.35 Å. The overall fol...
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| 主要な著者: | , , , , , , , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Biochemistry and Molecular Biology
2010
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2857070/ https://ncbi.nlm.nih.gov/pubmed/20164176 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.084509 |
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