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Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy.

Authors
  • Jue, T
  • La Mar, G N
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Mar 15, 1984
Volume
119
Issue
2
Pages
640–645
Identifiers
PMID: 6712648
Source
Medline
License
Unknown

Abstract

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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