Ph and temperature
Temperature is not a factor that directly promotes oxygen binding to and dissociation from hemoglobin. The main factors that influence this process are partial pressure of oxygen, pH, and the presence of other molecules such as carbon dioxide or 2,3-bisphosphoglycerate.
You have Iron atoms in hemoglobin. This atom is the binding site for oxygen in case of hemoglobin.
Hemoglobin cooperativity is a process where the binding of one oxygen molecule to a hemoglobin molecule makes it easier for other oxygen molecules to bind. This means that as more oxygen molecules bind to hemoglobin, the affinity for oxygen increases, allowing hemoglobin to efficiently transport oxygen in the bloodstream.
A negative feedback mechanism is a system to return a disruption in homeostasis back to homeostasis.A positive feedback mechanism is a system to reinforce or perpetuate a disruption in homeostasis.The oxyhemoglobin dissociation curve represents the Partial pressure in oxygen that will be saturated in the amount of hemoglobin.This curve represents a positive feedback because the binding of Oxygen to hemoglobin facilitates more binding of oxygen to hemoglobin (you can see this in the rapid rise in saturation from 10-40 mm Hg) until it reaches 60 mm Hg where it is somewhat completely saturated
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.
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.
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.
As it shifts to the right, it means that haemoglobin has a lesser affinity for oxygen
The oxygen-haemoglobin dissociation curve, also spelled oxygen-hemoglobin dissociation curve, plots the proportion of hemoglobin in its saturated form on the vertical axis against the prevailing oxygen tension on the horizontal axis. The oxyhemoglobin dissociation curve is an important tool for understanding how our blood carries and releases oxygen. Specifically, the oxyhemoglobin dissociation curve relates oxygen saturation (SO2) and partial pressure of oxygen in the blood (PO2), and is determined by what is called "hemoglobin's affinity for oxygen"; that is, how readily hemoglobin acquires and releases oxygen molecules into the fluid that surrounds it. found on wikipedia
Hemoglobin
Hemoglobin on red blood cells.
Oxygen has two binding sites in a hemoglobin molecule: one on each of the two alpha-beta dimers. This allows each hemoglobin molecule to bind and carry up to four oxygen molecules.