Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy.
- Published Article
Biochemical and biophysical research communications
- Publication Date
Mar 15, 1984
The number of 2,4-H signals of met-cyano and deoxy deuteroheme-reconstituted sperm whale Mb are shown to reflect the known degree of heme rotational disorder in this modified protein. Using these unique spectral windows for the 2,4-H signals, we show that both horse and human Hb reconstituted with deuteroheme exhibit significant molecular heterogeneity which is consistent with approximately 20% heme rotational disorder within each subunit.
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The corresponding record at NLM can be accessed at https://www.ncbi.nlm.nih.gov/pubmed/6712648