iron doesnt oxidize when oxygen binds to haemoglobin. instead ion induced dipole attraction is present between iron and oxygen.
source: my teacher and there's a bit about this on wikipedia. search for haemoglobin there.
JAWAD REHMAN
M A STUDENT
In formation of oxy-hemoglobin, oxygen does not combine with two positive
valences of the ferrous iron in the hemoglobin molecule. Instead, it binds loosely with
one of the six "coordination" valences of the iron atom. This is an extremely loose bond
so that combination is reversible. Furthermore, the oxygen does not become ionic oxygen but is carried as molecular oxygen to the tissue where it is released into the tissue fluids in the form of dissolved molecular oxygen rather than ionic oxygen. This explains why blood does not rust despite having the all necessary substrates for the formation of the rust.
Tahi
practically no difference. In both the hemoglobin has the same job, bonding with oxygen.
Hemoglobin
True
zax oxidize
Myoglobin and hemoglobin are structurally similar proteins, with around 20% sequence similarity. They both contain heme groups that bind oxygen, but hemoglobin is found in red blood cells and is responsible for transporting oxygen, while myoglobin is found in muscle tissue and is involved in storing and transporting oxygen within muscles.
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.
Anemia
Oxidize
This is a good question! Fetus gets the oxygen from the placenta. In case of the placenta, the blood from the mother and fetus comes in contact with each other. Here both the bloods are not mixed up and separated by thin membrane. Fetus needs very high quantity of the oxygen for the growth. So fetus has got more hemoglobin to extract more oxygen from the blood of mother. After the birth, this extra hemoglobin diminishes with time.
Hemoglobin is a protein and it has an iron ion that can attract an oxygen molecule to it. Both proteins and iron can be found in food.
The iron molecule (that's the hemo- in hemoglobin) gains and/or loses an oxygen molecule. The protein part (that's the globin) changes shape a bit. Both changes are very reversible and requires little energy.
This is tigarvin Found an answer in this website: http://www.ginfo.pl Hemoglobin Hope (beta (H14)136gly leads to asp), a mildly unstable variant, was found to have decreased oxygen affinity, a normal Bohr effect and diminished cooperativity . Decreased oxygen affinity of hemoglobin Hope may explain the previous failure to find an appropriate response to hemolysis in individuals studied who were heterozygous for both hemoglobin Hope and sickle hemoglobin. Salt bridge formation between NA1 valine and H14 aspartic acid may stabilize the beta Hope subunit in its deoxy form thus producing intrinsically low oxygen affinity and reduced cooperativity. need a better answer