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Blood, 1 April 2006, Vol. 107, No. 7, pp. 2602-2604.
Prepublished online as a Blood First Edition Paper on December 8, 2005; DOI 10.1182/blood-2005-10-4104.
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Submitted October 14, 2005
Accepted November 28, 2005
Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the beta subunit of hemoglobin
Kris T Huang, Ivan Azarov, Swati Basu, Jinming Huang, and Daniel B Kim-Shapiro*
Department of Biomedical Engineering, Wake Forest University School of Medicine, Winston-Salem, NC, USA
Department of Physics, Wake Forest University, Winston-Salem, NC, USA
Department of Chemistry, Wake Forest University, Winston-Salem, NC, USA
Department of Biomedical Engineering, Wake Forest University School of Medicine, Winston-Salem, NC, USA; Department of Physics, Wake Forest University, Winston-Salem, NC, USA
* Corresponding author; email: shapiro{at}wfu.edu.
The SNO-Hb hypothesis holds that heme-bound nitric oxide (NO) present in the beta subunits of T-state hemoglobin (Hb) will be transferred to the  -93 cysteine upon conversion to R-state Hb, thereby forming SNO-Hb. A deficiency in the ability of Hb to facilitate this intramolecular transfer has recently been purported to play a role in pulmonary hypertension and sickle cell disease. We prepared deoxygenated Hb samples with small amounts of heme bound NO and then oxygenated the samples. Electron Paramagnetic Resonance (EPR) spectroscopy was used to (1) determine the concentration of iron nitrosyl Hb (Fe-NO Hb), (2) show that the NO is evenly distributed among alpha and beta subunits, and (3) show that the Hb undergoes a change in its quaternary state (T to R) upon oxygenation. We did not observe a decrease in the concentration of Fe-NO Hb upon oxygenation which is inconsistent with the prediction of the SNO-Hb hypothesis.
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