As Red Cells Become Oxygenated in the Lungs, a Nitric Oxide (NO) Group is Covalently Bound to the Highly Conserved Cys93 Residue in the ß-Chain of Hemoglobin. In this high oxygen affinity state (the relaxed, R-state), SNO-Hgb is unreactive, but upon Hgb deoxygenation in the periphery and the consequent transition to the low oxygen affinity state (the tense, T-state), SNO-Hgb can react with red cell thiols (e.g., glutathione [GSH] or anion exchanger-1 [AE-1]) via transnitrosation and thereby transmit a vasodilatory signal (RSNO) out of the red cell.

As Red Cells Become Oxygenated in the Lungs, a Nitric Oxide (NO) Group is Covalently Bound to the Highly Conserved Cys93 Residue in the ß-Chain of Hemoglobin. In this high oxygen affinity state (the relaxed, R-state), SNO-Hgb is unreactive, but upon Hgb deoxygenation in the periphery and the consequent transition to the low oxygen affinity state (the tense, T-state), SNO-Hgb can react with red cell thiols (e.g., glutathione [GSH] or anion exchanger-1 [AE-1]) via transnitrosation and thereby transmit a vasodilatory signal (RSNO) out of the red cell.

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