Hemoglobin A.
(4)deoxyhemoglobinA molecule is a molecule which consists of four heme mechanisms(hereinafter reffered to as "heme").
It's known that although each heme is far enough apart, due to having a transmission mechanism to exchange information with each other, it exerts cooperativity.
See "The first thermodynamics in the world with regard to hemoglobin (11)." and ought to know my opinion on the hemoglobin's cooperativity.
porphyrin ring
Since ferrous ions in (2)oxyhemoglobinA fits in the porphyrin ring plane of the heme, the porphyrin annulus plane is planar.
Since ferrous ions in (4)deoxyhemoglobinA doesn't fit in the porphyrin ring plane of the heme, the porphyrin annulus plane is not planar.
Ferrous ion to which an oxygen molecule coordinates is smaller in low spin type, and ferrous ion to which an oxygen molecule dose not coordinate is larger in high spin type.
The information about planarity in one heme is transmitted to other heme in the same (4)deoxyhemoglobinA molecule, it exerts cooperativity due to promoting desorptions of oxygen molecule in the same direction.
Ferrous ion in (2)oxyhemoglobinA is located in the center of the octahedron.
Ferrous ion in (4)deoxyhemoglobinA is located inside the the porphyrin ring plane(opposite where an oxygen molecule coordinates).
the variation of pH value
In the human body, the blood in the capillaries of the alveoli of the lungs are relatively basic, in the capillaries of the terminal tissues of the body are relatively acidic.
Human blood is in the range contains neutral zone, and the width of pH value is about 1.0.
In the variation of pH value within that range, the energy of (2)oxyhemoglobinA is high in the acidic range and low in the basic range.
The energy of deoxyhemoglobinA is low in the acidic range and high in the basic range.
The energy of (2)oxyhemoglobinA is low with stable state in capillaries of the alveoli of the lungs which the blood is basic reletively in.
In capillaries of the alveoli of the lungs, the (4)deoxyhemoglobinA high energy relatively changes into the (2)oxyhemoglobinA.
The energy of (2)oxyhemoglobinA is high with unstable state in the capillaries of terminal tissues of the body which the blood is acidic reletively in.
Desorbing oxygen molecule, (2)oxyhemoglobinA changes into (4)deoxyhemoglobinA, due to the low energy state of (4)deoxyhemoglobinA.
mioglibin
Futher more, mioglibin (hereinafter reffered to as "deoxymioglobin", in addition the material which is coodinated by oxygen molecule to deoxymioglobin reffered to as "oxymioglobin" ) is waiting there and reacts with oxygen molecule taking it into the molecule as a coodinate, and it becomes oxymioglobin with stable energy state.
Due to a series of concerted transfers of oxygen molecule, the reaction system achieves a stable state with low energy.
Oxygen molecules in oxymioglobins are used in metabolic process.
In a spontanious process, a state with high energy changes into one with low energy.
At last oxygen molecules have been delivered to the terminal tissues of one's body.
The first thermodynamics in the world with regard to hemoglobin (11). Hemoglobin cooperativety
https://wishikawa.hatenablog.com/entry/2024/01/29/000000?_gl=1*cwvrjh*_gcl_au*Mzc1MTQ1NDAzLjE3MDY5OTg5MTM.
