[HTML][HTML] Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: implications for interactions of nitric oxide with normal and sickle red blood cells
C Bonaventura, CH Taboy, PS Low, RD Stevens… - Journal of Biological …, 2002 - ASBMB
S-Nitrosated hemoglobin is remarkably stable and can be cycled between deoxy,
oxygenated, or oxidized forms without significant loss of NO. Here we show thatS-nitrosation
of adult human hemoglobin (Hb A 0) or sickle cell Hb (Hb S) results in an increased ease of
anaerobic heme oxidation, while anions cause redox shifts in the opposite direction. The
negatively charged groups of the cytoplasmic domain of Band 3 protein also produce an
allosteric effect on S-nitrosated Hb. Formation and deoxygenation of a SNO-Hb/Band 3 …
oxygenated, or oxidized forms without significant loss of NO. Here we show thatS-nitrosation
of adult human hemoglobin (Hb A 0) or sickle cell Hb (Hb S) results in an increased ease of
anaerobic heme oxidation, while anions cause redox shifts in the opposite direction. The
negatively charged groups of the cytoplasmic domain of Band 3 protein also produce an
allosteric effect on S-nitrosated Hb. Formation and deoxygenation of a SNO-Hb/Band 3 …