NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin
Compared with free heme, the proteins hemoglobin (Hb) and myoglobin (Mb) exhibit greatly enhanced affinity for oxygen relative to carbon monoxide. This physiologically vital property has been attributed to either steric hindrance of CO or stabilization of O(2) binding by a hydrogen bond with the dis...
שמור ב:
| הוצא לאור ב: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
National Academy of Sciences
2000
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC27028/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10962034/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.190254697 |
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