Oxygen-15-oxyhemoglobin

Oxygen solubility Oxygen tents Oxygen transfer Oxygen transfer rate Oxygen transport Oxyhalide Oxyhemoglobin... 

In addition to COg, Cl and BPG also bind better to deoxyhemoglobin than to oxyhemoglobin, causing a shift in equilibrium in favor of Og release. These various effects are demonstrated by the shift in the oxygen saturation curves for Hb in the presence of one or more of these substances (Figure 15.35). Note that the Og-binding curve for Hb + BPG + COg fits that of whole blood very well. 

The sixth coordination position of Fe2+ in heme is occupied by a water molecule that can be replaced reversibly by oxygen to give a derivative known as oxyhemoglobin, which has the bright red color characteristic of arterial blood. 

Lungs saturated with oxygen so the shift is to oxyhemoglobin formation. Tissues low in oxygen, so in venal blood, the shift is to hemoglobin formation. 

The P02 of blood is the major factor determining the amount of oxygen chemically combined with hemoglobin, or the percent of hemoglobin saturation. The relationship between these two variables is illustrated graphically by the oxyhemoglobin dissociation curve (see Figure 17.6). This relationship is not... 

The toxicity of dapsone is due to the cytochrome P-450-catalyzed oxygenation leading to iV-hydroxydapsone. This major metabolite enters red cells and is co-oxidized with oxyhemoglobin to generate a nitroso derivative and methemoglobin148. 

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