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• W2068170470 abstract "Abstract The SNO-Hb hypothesis holds that heme-bound nitric oxide (NO) present in the β subunits of T-state hemoglobin (Hb) will be transferred to the β-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 α and β 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." @default.
• W2068170470 created "2016-06-24" @default.
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• W2068170470 date "2006-04-01" @default.
• W2068170470 modified "2023-10-18" @default.
• W2068170470 title "Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the β subunit of hemoglobin" @default.
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• W2068170470 doi "https://doi.org/10.1182/blood-2005-10-4104" @default.
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