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
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.
Red blood cells are packed with a chemical compound called hemoglobin, which has the ability to both absorb and release oxygen molecules.
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
Blood has a chemical in it called hemoglobin, attached to the red blood cells. Certain molecules, including oxygen, are react quite strongly with hemoglobin. The lungs end in tiny little bubble-like membranes called alveoli. These are surrounded by tiny blood vessels called capillaries, which connect the pulmonary artery and pulmonary vein. (These carry unoxygenated blood from heart to lungs, and oxygenated blood back into the heart, respectively.) The membranes are permeable to both carbon dioxide and oxygen. Carbon dioxide gets released into the air within the alveoli (after being produced in individual cells and collected in the rest of the circulatory system), while oxygen slips over from the air into the blood and reacts with the hemoglobin. From there, it's carried back to your heart, and then out to the rest of the body to be used in cellular respiration (the most fundamental function of cells; essentially the power plant for the cell) (The other noteworthy chemical that reacts with hemoglobin similarly is carbon monoxide, an odorless gas. It attaches to hemoglobin so strongly that the body can't remove it (there's some kind of reaction at the other end that makes hemoglobin release oxygen - it doesn't work with carbon monoxide). If you breathe in too much, all of your blood has carbon monoxide attached, and you effectively suffocate. The only way you can tell its happening is that you begin to feel inexplicably tired.)