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The red crystalline pigment formed in blood by the combination of oxygen and hemoglobin, without the oxidation of iron.



the oxygenated form of hemoglobin (HbO2) that results from the reversible combination of oxygen and reduced hemoglobin (Hb). Oxyhemoglobin carries O2 from the respiratory organs to the tissues and imparts a bright red color to arterial blood. The O2 molecule is bonded to Hb by the Fe2+ atom in heme; the valence of Fe2+ remains unchanged during this process, that is, no actual oxidation takes place. The combination of O2 with one of the four heme groups alters the three dimensional Hb structure and the affinity of the remaining heme groups for O2.

The formation and dissociation of oxyhemoglobin are influenced by several factors, including CO2 concentration and pH. The structure of heme in the Hb molecule is the same for all animals, but the protein fraction—globin—differs from species to species in size, amino-acid composition, and physical properties. The structure of globin is another factor that affects the affinity of Hb for O2. Species differences in globin structure are associated with natural habitat: in general, an increase in the supply of available O2 decreases the affinity of Hb for O2 and consequently increases the partial pressure of O2; this increase is necessary to effect Hb saturation and formation of HbO2. For example, the Hb of land animals exhibits a lower affinity for O2 than that of aquatic animals; fishes that inhabit running water have Hb with a lower O2 affinity than species dwelling in stagnant water. A given species may even have several Hb types, which replace each other during ontogenesis; for example, HbO2 forms more readily in the human fetus than in the adult.


Prosser, L., and F. Brown. Sravnitel’naia fiziologiia zhivotnykh. Moscow, 1967. Pages 238–79. (Translated from English.)
Korzhuev, P. A. “Problema oksigenatsii gemoglobina.” Uspekhi fiziologicheskikh nauk, 1973, vol. 4, no. 3.
References in periodicals archive ?
where Hb[O.sub.2] is the concentration of oxygenated hemoglobin and Hb is the concentration of deoxygenated hemoglobin [12].
The reaction takes place with oxygenated hemoglobin in R conformation [14].
This negative trend implied an overall reduction in the detrusor blood volume and the availability of oxygenated hemoglobin over the course of voiding.
The sampling rate was approximately 11.76 Hz; hence, the time gap between sample points of each detector for oxygenated hemoglobin (HbO) and deoxygenated hemoglobin (HbR) signals was 85.03 ms.
Oxygenated hemoglobin in blood absorbs light at 660mn which is red light.
Changes in the concentration of the chromophores oxygenated hemoglobin "[DELTA][O.sub.2]Hb" and deoxyhemoglobin "[DELTA]HHb" were calculated by the modified Beer-Lambert equation in [mu]M = [10.SUP.[-6]] mol units (Delpy et al.
They are developing a method to monitor both total hemoglobin and oxygenated hemoglobin at specific sites in the body.
Specifically, this approach determines the ratio of hemoglobin that is still carrying oxygen (i.e., oxygenated hemoglobin) to hemoglobin that has already delivered its oxygen to the tissues (i.e., deoxygenated hemoglobin).