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A Model for the Flexibility of the Distal Histidine in Dehaloperoxidase-Hemoglobin A Based on X-ray Crystal Structures of the Carbon Monoxide Adduct
[Image: see text] Dehaloperoxidase hemoglobin A (DHP A) is a multifunctional hemoglobin that appears to have evolved oxidative pathways for the degradation of xenobiotics as a protective function that complements the oxygen transport function. DHP A possesses at least two internal binding sites, one...
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| Asıl Yazarlar: | , , |
|---|---|
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American
Chemical Society
2014
|
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4203366/ https://ncbi.nlm.nih.gov/pubmed/24670063 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi5001905 |
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