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...

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Detalhes bibliográficos

Publicado no:	Proc Natl Acad Sci U S A
Principais autores:	Lukin, Jonathan A., Simplaceanu, Virgil, Zou, Ming, Ho, Nancy T., Ho, Chien
Formato:	Artigo
Idioma:	Inglês
Publicado em:	National Academy of Sciences 2000
Assuntos:	Biological Sciences
Acesso em linha:	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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