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You have Iron atoms in hemoglobin. This atom is the binding site for oxygen in case of hemoglobin.
number of red blood cells
This is called the Bohr effect where a increase in pC02 which decrease the pH leads to a decreased affinity of hemoglobin to oxygen. This means that hemoglobin unloads oxygen in areas where pC02 is high e.g. active tissue and that the binding coefficient of hemoglobin is highest in the lung where pC02 is negligible.
It is not the fourth one specifically that binds easier, O2 is a positive allosteric effector (activator) of Haemoglobin and the binding of O2 facilitates further binding of O2. I'm not sure why this is though.
The affinity of CO for the O2 binding sites is 200X increased than that of O2. At the same time, CO binding does not respond to declining PaO2 levels. Therefore the remaining O2 remain more avidly bound and unload slower than normal, thus resulting in a leftward shift.
You have Iron atoms in hemoglobin. This atom is the binding site for oxygen in case of hemoglobin.
Because the binding of oxygen to hemoglobin is cooperative, i.e. it exhibits positive cooperativity. This essentially means that the binding of the first molecule of oxygen facilitates the binding of the second, and so on.
Ph and temperature
Hemoglobin
Hemoglobin on red blood cells.
All hemoglobin has something called the Bohr effect, which is a negative effect of binding oxygen by hemoglobin in the presence of acid. This effect is some what exaggerated in diving mammals.
after one oxygen molecule binds to hemoglobin, it is easier for the other molecules to bind to the hemoglobin. this is known as cooperative binding.
The Bohr effect and cooperative binding of oxygen to hemoglobin is what makes it an effective carrier of oxygen from the lungs to the peripheral tissues. What is cooperative binding? The first oxygen bind less strongly to oxygen then does the subsequent oxygen molecules (hemoglobin has four binding zones for oxygen). This means that the binding curve is fairly steep. The Bohr effect is a negative effect on binding of oxygen by hemoglobin in the presence of increased pH. Since peripheral tissues release C02 it increases the local pH releasing the oxygen. After the first oxygen is released the remaining oxygen molecules are quickly disassociated from hemoglobin thus delivering the oxygen to the tissue in need of oxygen.
Hemoglobin contains a heme group with an Iron ion attached to it. The iron is what binds to O2.
saturation
Look up a hemoglobin oxygen-binding curve, that will tell you.
number of red blood cells