Nitric oxide (NO) activates soluble guanylyl cyclase in smooth muscle cells to induce
vasodilation in the vasculature. However, as hemoglobin (Hb) is an effective scavenger of …

It has been reported that free hemoglobin (Hb) reacts with NO at an extremely high rate (K
Hb∼ 10 7 m− 1 s− 1) and that the red blood cell (RBC) membrane is highly permeable to …

The process of NO transfer into erythrocytes (RBCs) is of critical biological importance
because it regulates the bioavailability and diffusional distance of endothelial-derived NO. It …

Nitrite has long been known to be vasoactive when present at large concentrations but it
was thought to be inactive under physiological conditions. Surprisingly, we have recently …

It is generally believed that the erythrocyte membrane is highly permeable to nitric oxide
(NO). To prevent NO from freely entering and being scavenged by the red blood cell (RBC) …

The reaction rate between nitric oxide and intraerythrocytic hemoglobin plays a major role in
nitric oxide bioavailability and modulates homeostatic vascular function. It has previously …

Encapsulation of hemoglobin (Hb) within red blood cells (RBCs) preserves nitric oxide (NO)
bioactivity. With encapsulation, millimolar concentrations of Hb quench only a fraction of NO …

Nitric oxide (NO) acts as a smooth muscle relaxation factor and plays a crucial role in
maintaining vascular homeostasis. NO is scavenged rapidly by hemoglobin (Hb). However …

The ability of oxyhemoglobin to inhibit nitric oxide (NO)-dependent activation of soluble
guanylate cyclase and vasodilation provided some of the earliest experimental evidence …

Background: Nitrosation of a conserved cysteine residue at position 93 in the hemoglobin β
chain (β93C) to form S-nitroso (SNO) hemoglobin (Hb) is claimed to be essential for export …