Nitric oxide binding to oxygenated hemoglobin under physiological conditions.
Biochim Biophys Acta
; 1568(3): 252-60, 2001 Dec 19.
Article
in En
| MEDLINE
| ID: mdl-11786232
ABSTRACT
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Hemoglobins
/
Oxyhemoglobins
/
Erythrocytes
/
Nitric Oxide
Limits:
Humans
Language:
En
Journal:
Biochim Biophys Acta
Year:
2001
Document type:
Article
Affiliation country:
United States