Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1568, Issue 3, Pages 252-260Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0304-4165(01)00227-6
Keywords
hemoglobin; nitric oxides; EPR spectroscopy; absorption; allostery
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Funding
- NHLBI NIH HHS [HL58091, R29 HL058091] Funding Source: Medline
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We have added nitric oxide (NO) to hemoglobin in 0.1 M and 0.01 M phosphate buffers as well as to whole blood, all as a function of hemoglobin oxygen saturation. We found that in all these conditions, the amount of nitrosyl hemoglobin (HbNO) formed follows a model where the rates of HbNO formation and methemoglobin (metHb) formation (via hemoglobin oxidation) are independent of oxygen saturation. These results contradict those of an earlier report where, at least in 0.01 M phosphate, an elevated amount of HbNO was formed at high oxygen saturations. A radical rethink of the reaction of oxyhemoglobin with NO under physiological conditions was called for based on this previous proposition that the primary product is HbNO rather than metHb and nitrate. Our results indicate that no such radical rethink is called for. (C) 2001 Elsevier Science B.V. All rights reserved.
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