Hemoglobin is perhaps the most intensively studied of the biologically important molecules. Much is known of its structure, its function, and its regulation. In addition to well-characterized processes of oxygen, carbon dioxide, and carbon monoxide transport, new data suggest a key role of hemoglobin as a carrier of nitric oxide. In this review, we describe the basis of this interaction, as well as its clinical relevance to such problems as acute respiratory distress syndrome, percutaneous transluminal coronary angioplasty, and transplant allograft survival.
Nitric oxide (NO) is derived from exogenous and endogenous sources. While S-nitrosohemoglobin increases blood flow by delivery of NO to vascular smooth muscle, the heme portion of hemoglobin scavenges NO, resulting in vasoconstriction. Free radicals react with NO, forming cytotoxic peroxynitrite.
Oxygenated S-nitrosohemoglobin (SNO-HbO2) is formed in the lungs. In the peripheral vasculature, both nitric oxide (NO) and oxygen (O2) are released. Nitric oxide delivery causes vasodilation and counteracts scavenging of NO by hemoglobin (HbFe2+-NO) to ensure oxygen delivery matches oxygen demand.
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