Combustion
Oxygen.
Fluorine has the highest electron affinity because it has a small atomic size and high effective nuclear charge, which results in a strong attraction between the nucleus and incoming electrons. This strong attraction allows fluorine to readily accept an additional electron and achieve a stable electron configuration.
In anemia, 2,3-DPG (2,3-diphosphoglycerate) levels are typically elevated. This compound decreases the affinity of hemoglobin for oxygen, helping to release oxygen to the tissues. Consequently, oxygen delivery to tissues may be improved despite the lower hemoglobin levels in anemia.
It has high affinity for electrons.
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.
Oxygen.
Oxygen: It has higher electronegativity than any of the others listed.
Red blood cells have the highest affinity for both oxygen and carbon dioxide. This is due to the presence of the protein hemoglobin in red blood cells, which binds to oxygen and carbon dioxide molecules. Hemoglobin helps transport oxygen from the lungs to tissues and carries carbon dioxide away from the tissues to be exhaled from the lungs.
As it shifts to the right, it means that haemoglobin has a lesser affinity for oxygen
chlorine has the highest electron affinity
Fluorine has the highest electron affinity because it has a small atomic size and high effective nuclear charge, which results in a strong attraction between the nucleus and incoming electrons. This strong attraction allows fluorine to readily accept an additional electron and achieve a stable electron configuration.
Sodium, when exposed to air has a great affinity for oxygen, such that it bursts into flame
Myoglobin has a high affinity for oxygen due to the heme group present within its structure, which can form strong bonds with oxygen molecules. The heme group has a distal histidine residue that stabilizes the bound oxygen molecule, contributing to the high affinity of myoglobin for oxygen. Additionally, myoglobin has a hydrophobic pocket that further enhances its ability to bind oxygen tightly.
Haemoglobine combines with oxygen to form oxihaemoglobine
In anemia, 2,3-DPG (2,3-diphosphoglycerate) levels are typically elevated. This compound decreases the affinity of hemoglobin for oxygen, helping to release oxygen to the tissues. Consequently, oxygen delivery to tissues may be improved despite the lower hemoglobin levels in anemia.
The affinity of hemoglobin for CO is roughly 20,000 times greater than that of oxygen in vitro. In vivo, the affinity of hemoglobin for CO is roughly 200-225 greater than that of oxygen. ------------------------------------------------------------------------------------------------- O2 has stronger bond than CO. Therefore, the oxygen in CO loves the iron in the hemoglobin as iron ends with two electrons which complete the 6 electrons in the oxygen. In vivo, the affinity of hemglobin for CO is about 153 from 141x153/141. by amin elsersawi
It has high affinity for electrons.