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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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PLENARY PAPERS

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

From the Department of Biomedical Engineering, Wake Forest University School of Medicine; and Department of Physics and Department of Chemistry, Wake Forest University, Winston-Salem, NC.

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 beta-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 on oxygenation, which is inconsistent with the prediction of the SNO-Hb hypothesis.


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