Modulation of nitric oxide affinity by amino acid residues in the pocket of the β-chains

C. Fronticelli, N. Shoaee

Research output: Contribution to journalConference articlepeer-review


Vasoactivity represents a major concern for the in vivo use of cell free hemoglobin believed to result from the interaction of hemoglobin with the endothelium-derived relaxing factor (EDRF). Strong evidence shows that EDRF is in fact nitric oxide (NO). The high affinity of NO for hemoglobin is due to its extremely low dissociation reaction. An increase in NO dissociation will result in a decreased affinity for NO. These indicate that the affinity for NO can be affected by amino acid substitutions in the heme pocket.

Original languageEnglish (US)
Pages (from-to)A100
JournalArtificial Cells, Blood Substitutes, and Immobilization Biotechnology
Issue number5
StatePublished - Nov 1 1994
Externally publishedYes
EventProceedings of the 11th Congress of the International Society for Artificial Cells, Blood Substitutes and Immobilization Biotechnology, (ISABI) - Boston, MA, USA
Duration: Jul 24 1994Jul 27 1994

ASJC Scopus subject areas

  • Biotechnology
  • Biomedical Engineering


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