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Controlling Conformational Flexibility of an O(2)-binding H-NOX Domain()
Heme Nitric oxide and/or OXygen binding (H-NOX) domains have provided a novel scaffold to probe ligand affinity in hemoproteins. Mutation of isoleucine 5, a conserved residue located in the heme-binding pocket of the H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX), was carried out to e...
Tallennettuna:
| Päätekijät: | , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2011
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3153587/ https://ncbi.nlm.nih.gov/pubmed/21721586 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi200788x |
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